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PloS one2009; 4(5); e5726; doi: 10.1371/journal.pone.0005726

Latherin: a surfactant protein of horse sweat and saliva.

Abstract: Horses are unusual in producing protein-rich sweat for thermoregulation, a major component of which is latherin, a highly surface-active, non-glycosylated protein. The amino acid sequence of latherin, determined from cDNA analysis, is highly conserved across four geographically dispersed equid species (horse, zebra, onager, ass), and is similar to a family of proteins only found previously in the oral cavity and associated tissues of mammals. Latherin produces a significant reduction in water surface tension at low concentrations (< or = 1 mg ml(-1)), and therefore probably acts as a wetting agent to facilitate evaporative cooling through a waterproofed pelt. Neutron reflection experiments indicate that this detergent-like activity is associated with the formation of a dense protein layer, about 10 A thick, at the air-water interface. However, biophysical characterization (circular dichroism, differential scanning calorimetry) in solution shows that latherin behaves like a typical globular protein, although with unusual intrinsic fluorescence characteristics, suggesting that significant conformational change or unfolding of the protein is required for assembly of the air-water interfacial layer. RT-PCR screening revealed latherin transcripts in horse skin and salivary gland but in no other tissues. Recombinant latherin produced in bacteria was also found to be the target of IgE antibody from horse-allergic subjects. Equids therefore may have adapted an oral/salivary mucosal protein for two purposes peculiar to their lifestyle, namely their need for rapid and efficient heat dissipation and their specialisation for masticating and processing large quantities of dry food material.
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Publication Date: 2009-05-29 PubMed ID: 19478940PubMed Central: PMC2684629DOI: 10.1371/journal.pone.0005726Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research focuses on latherin, a protein found in the sweat and saliva of horses, and its role in thermoregulation. The study provides insight into latherin’s ability to decrease water surface tension, and potential in facilitating illustrious cooling in these animals. Moreover, the protein’s sequence remains consistent across multiple equid species and shares similarities with proteins found in other mammals’ oral areas.

Latherin’s Properties & Function

  • The research indicates that latherin, a protein found in horse sweat and saliva, has a key role in regulating body temperature. It is unusual in that it is a surface-active, non-glycosylated protein and is highly conserved across different species.
  • Latherin lowered water surface tension at low concentrations, suggesting it serves as a wetting agent, helping enhance the efficiency of evaporative cooling. Horses, particularly, have a necessity for swift and effective heat dissipation due to their active lifestyle.

Protein Behaviour & Presence in Equids

  • Biophysical characterization unveiled latherin behaves like a standard globular protein in solution, with atypical intrinsic fluorescence characteristics. These characteristics suggest significant conformational change or unfolding of the protein is necessary for forming the air-water interfacial layer.
  • The presence of latherin transcripts were exclusively found in horse skin and salivary glands. Its sequence is identical across geographically diverse equid species, including horses, zebras, onagers, and donkeys.

Relevance to Allergic Reactions & Application in Other Species

  • The research also discovered that recombinantly produced latherin is a target of IgE antibodies from individuals allergic to horses. Hence, latherin likely contributes to allergenic reactions in sensitive individuals.
  • Interestingly, latherin is similar to a family of proteins found in oral cavities and related tissues of other mammals. The researchers propose that these species may have adapted an oral/salivary mucosal protein for facilitating their need for heat dissipation and processing large quantities of dry food.

Cite This Article

APA
McDonald RE, Fleming RI, Beeley JG, Bovell DL, Lu JR, Zhao X, Cooper A, Kennedy MW. (2009). Latherin: a surfactant protein of horse sweat and saliva. PLoS One, 4(5), e5726. https://doi.org/10.1371/journal.pone.0005726

Publication

PloS one
ISSN: 1932-6203
NlmUniqueID: 101285081
Country: United States
Language: English
Volume: 4
Issue: 5
Pages: e5726
PII: e5726

Researcher Affiliations

McDonald, Rhona E
  • Ecology and Evolutionary Biology, Faculty of Biomedical and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
Fleming, Rachel I
    Beeley, John G
      Bovell, Douglas L
        Lu, Jian R
          Zhao, Xiubo
            Cooper, Alan
              Kennedy, Malcolm W

                MeSH Terms

                • Allergens
                • Amino Acid Sequence
                • Animals
                • Biophysical Phenomena
                • Fatty Acid-Binding Proteins
                • Fluorescence
                • Horses / metabolism
                • Molecular Sequence Data
                • Neutrons
                • Proteins / chemistry
                • Proteins / genetics
                • Proteins / metabolism
                • Recombinant Proteins / chemistry
                • Recombinant Proteins / genetics
                • Recombinant Proteins / metabolism
                • Saliva / metabolism
                • Sequence Analysis, Protein
                • Sequence Homology, Amino Acid
                • Surface Tension
                • Surface-Active Agents / chemistry
                • Surface-Active Agents / metabolism
                • Sweat / metabolism
                • Transcription, Genetic
                • Tryptophan / metabolism

                Grant Funding

                • Wellcome Trust
                • GR070994MA / Wellcome Trust

                Conflict of Interest Statement

                The authors have declared that no competing interests exist.

                References

                This article includes 53 references
                1. McEwan Jenkinson D, Elder HY, Bovell DL. Equine sweating and anhidrosis Part 1--equine sweating.. Vet Dermatol 2006 Dec;17(6):361-92.
                  pubmed: 17083570doi: 10.1111/j.1365-3164.2006.00545.xgoogle scholar: lookup
                2. Possmayer F, Nag K, Rodriguez K, Qanbar R, Schürch S. Surface activity in vitro: role of surfactant proteins.. Comp Biochem Physiol A Mol Integr Physiol 2001 May;129(1):209-20.
                  pubmed: 11369545doi: 10.1016/s1095-6433(01)00317-8google scholar: lookup
                3. Wright JR. Immunoregulatory functions of surfactant proteins.. Nat Rev Immunol 2005 Jan;5(1):58-68.
                  pubmed: 15630429doi: 10.1038/nri1528google scholar: lookup
                4. McGuire JF. Surfactant in the middle ear and eustachian tube: a review.. Int J Pediatr Otorhinolaryngol 2002 Oct 21;66(1):1-15.
                  pubmed: 12363416doi: 10.1016/s0165-5876(02)00203-3google scholar: lookup
                5. Kankavi O, Ata A, Gungor O. Surfactant proteins A and D in the genital tract of mares.. Anim Reprod Sci 2007 Apr;98(3-4):259-70.
                  pubmed: 16621351doi: 10.1016/j.anireprosci.2006.03.009google scholar: lookup
                6. Kim JK, Kim SS, Rha KW, Kim CH, Cho JH, Lee CH, Lee JG, Yoon JH. Expression and localization of surfactant proteins in human nasal epithelium.. Am J Physiol Lung Cell Mol Physiol 2007 Apr;292(4):L879-84.
                  pubmed: 17209137doi: 10.1152/ajplung.00156.2006google scholar: lookup
                7. Kankavi O. Increased expression of surfactant protein A and D in rheumatoid arthritic synovial fluid (RASF).. Croat Med J 2006 Feb;47(1):155-61.
                  pmc: PMC2080374pubmed: 16489709
                8. Beeley JG, Eason R, Snow DH. Isolation and characterization of latherin, a surface-active protein from horse sweat.. Biochem J 1986 May 1;235(3):645-50.
                  pmc: PMC1146737pubmed: 3753435doi: 10.1042/bj2350645google scholar: lookup
                9. Hakanpää J, Linder M, Popov A, Schmidt A, Rouvinen J. Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A.. Acta Crystallogr D Biol Crystallogr 2006 Apr;62(Pt 4):356-67.
                  pubmed: 16552136doi: 10.1107/s0907444906000862google scholar: lookup
                10. Hakanpää J, Paananen A, Askolin S, Nakari-Setälä T, Parkkinen T, Penttilä M, Linder MB, Rouvinen J. Atomic resolution structure of the HFBII hydrophobin, a self-assembling amphiphile.. J Biol Chem 2004 Jan 2;279(1):534-9.
                  pubmed: 14555650doi: 10.1074/jbc.m309650200google scholar: lookup
                11. Hakanpää J, Szilvay GR, Kaljunen H, Maksimainen M, Linder M, Rouvinen J. Two crystal structures of Trichoderma reesei hydrophobin HFBI--the structure of a protein amphiphile with and without detergent interaction.. Protein Sci 2006 Sep;15(9):2129-40.
                  pmc: PMC2242604pubmed: 16882996doi: 10.1110/ps.062326706google scholar: lookup
                12. Clarkson JR, Cui ZF, Darton RC. Protein Denaturation in Foam.. J Colloid Interface Sci 1999 Jul 15;215(2):333-338.
                  pubmed: 10419668doi: 10.1006/jcis.1999.6256google scholar: lookup
                13. Singh P, Cameotra SS. Potential applications of microbial surfactants in biomedical sciences.. Trends Biotechnol 2004 Mar;22(3):142-6.
                  pubmed: 15036865doi: 10.1016/j.tibtech.2004.01.010google scholar: lookup
                14. Cameotra SS, Makkar RS. Recent applications of biosurfactants as biological and immunological molecules.. Curr Opin Microbiol 2004 Jun;7(3):262-6.
                  pubmed: 15196493doi: 10.1016/j.mib.2004.04.006google scholar: lookup
                15. Bendtsen JD, Nielsen H, von Heijne G, Brunak S. Improved prediction of signal peptides: SignalP 3.0.. J Mol Biol 2004 Jul 16;340(4):783-95.
                  pubmed: 15223320doi: 10.1016/j.jmb.2004.05.028google scholar: lookup
                16. Goubran Botros H, Poncet P, Rabillon J, Fontaine T, Laval JM, David B. Biochemical characterization and surfactant properties of horse allergens.. Eur J Biochem 2001 May;268(10):3126-36.
                  pubmed: 11358533doi: 10.1046/j.1432-1327.2001.02217.xgoogle scholar: lookup
                17. Bingle CD, LeClair EE, Havard S, Bingle L, Gillingham P, Craven CJ. Phylogenetic and evolutionary analysis of the PLUNC gene family.. Protein Sci 2004 Feb;13(2):422-30.
                  pmc: PMC2286710pubmed: 14739326doi: 10.1110/ps.03332704google scholar: lookup
                18. Bingle CD, Craven CJ. PLUNC: a novel family of candidate host defence proteins expressed in the upper airways and nasopharynx.. Hum Mol Genet 2002 Apr 15;11(8):937-43.
                  pubmed: 11971875doi: 10.1093/hmg/11.8.937google scholar: lookup
                19. Fenton MJ, Golenbock DT. LPS-binding proteins and receptors.. J Leukoc Biol 1998 Jul;64(1):25-32.
                  pubmed: 9665271doi: 10.1002/jlb.64.1.25google scholar: lookup
                20. Elsbach P, Weiss J. Role of the bactericidal/permeability-increasing protein in host defence.. Curr Opin Immunol 1998 Feb;10(1):45-9.
                  pubmed: 9523110doi: 10.1016/s0952-7915(98)80030-7google scholar: lookup
                21. Bingle CD, Craven CJ. Meet the relatives: a family of BPI- and LBP-related proteins.. Trends Immunol 2004 Feb;25(2):53-5.
                  pubmed: 15106612doi: 10.1016/j.it.2003.11.007google scholar: lookup
                22. Bingle CD, Gorr SU. Host defense in oral and airway epithelia: chromosome 20 contributes a new protein family.. Int J Biochem Cell Biol 2004 Nov;36(11):2144-52.
                  pubmed: 15313462doi: 10.1016/j.biocel.2004.05.002google scholar: lookup
                23. Bingle L, Wallace WA, Cross SS, High AS, Devine DA. Localisation of the putative mediator of host defence, SPLUNC1, in human tissues.. Journal of Pathology 2004;204:45A–45A.
                24. Egland KA, Vincent JJ, Strausberg R, Lee B, Pastan I. Discovery of the breast cancer gene BASE using a molecular approach to enrich for genes encoding membrane and secreted proteins.. Proc Natl Acad Sci U S A 2003 Feb 4;100(3):1099-104.
                  pmc: PMC298733pubmed: 12538848doi: 10.1073/pnas.0337425100google scholar: lookup
                25. LeClair EE, Nguyen L, Bingle L, MacGowan A, Singleton V, Ward SJ, Bingle CD. Genomic organization of the mouse plunc gene and expression in the developing airways and thymus.. Biochem Biophys Res Commun 2001 Jun 15;284(3):792-7.
                  pubmed: 11396972doi: 10.1006/bbrc.2001.5024google scholar: lookup
                26. Mulero JJ, Boyle BJ, Bradley S, Bright JM, Nelken ST, Ho TT, Mize NK, Childs JD, Ballinger DG, Ford JE, Rupp F. Three new human members of the lipid transfer/lipopolysaccharide binding protein family (LT/LBP).. Immunogenetics 2002 Aug;54(5):293-300.
                  pubmed: 12185532doi: 10.1007/s00251-002-0467-3google scholar: lookup
                27. Beamer LJ, Carroll SF, Eisenberg D. The BPI/LBP family of proteins: a structural analysis of conserved regions.. Protein Sci 1998 Apr;7(4):906-14.
                  pmc: PMC2143972pubmed: 9568897doi: 10.1002/pro.5560070408google scholar: lookup
                28. Eftink MR, Ghiron CA. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies.. Biochemistry 1976 Feb 10;15(3):672-80.
                  pubmed: 1252418doi: 10.1021/bi00648a035google scholar: lookup
                29. Eftink MR, Ghiron CA. Exposure of tryptophanyl residues and protein dynamics.. Biochemistry 1977 Dec 13;16(25):5546-51.
                  pubmed: 921949doi: 10.1021/bi00644a024google scholar: lookup
                30. Kennedy MW, Beauchamp J. Sticky-finger interaction sites on cytosolic lipid-binding proteins?. Cell Mol Life Sci 2000 Sep;57(10):1379-87.
                  pubmed: 11078017doi: 10.1007/pl00000623google scholar: lookup
                31. Eftink MR, Ghiron CA. Indole fluorescence quenching studies on proteins and model systems: Use of the efficient quencher succinimide.. Biochemistry 1984;23:3891–3899.
                32. Alston RW, Lasagna M, Grimsley GR, Scholtz JM, Reinhart GD, Pace CN. Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa.. Biophys J 2008 Mar 15;94(6):2288-96.
                  pmc: PMC2257903pubmed: 18065473doi: 10.1529/biophysj.107.116954google scholar: lookup
                33. Alston RW, Lasagna M, Grimsley GR, Scholtz JM, Reinhart GD, Pace CN. Peptide sequence and conformation strongly influence tryptophan fluorescence.. Biophys J 2008 Mar 15;94(6):2280-7.
                  pmc: PMC2257887pubmed: 18065477doi: 10.1529/biophysj.107.116921google scholar: lookup
                34. Mackenzie CD, Smith BO, Meister A, Blume A, Zhao X, Lu JR, Kennedy MW, Cooper A. Ranaspumin-2: structure and function of a surfactant protein from the foam nests of a tropical frog.. Biophys J 2009 Jun 17;96(12):4984-92.
                  pmc: PMC2712023pubmed: 19527658doi: 10.1016/j.bpj.2009.03.044google scholar: lookup
                35. Lu JR, Perumal S, Powers ET, Kelly JW, Webster JR, Penfold J. Adsorption of beta-hairpin peptides on the surface of water: a neutron reflection study.. J Am Chem Soc 2003 Apr 2;125(13):3751-7.
                  pubmed: 12656605doi: 10.1021/ja0292290google scholar: lookup
                36. Gregoire C, Rosinski-Chupin I, Rabillon J, Alzari PM, David B, Dandeu JP. cDNA cloning and sequencing reveal the major horse allergen Equ c1 to be a glycoprotein member of the lipocalin superfamily.. J Biol Chem 1996 Dec 20;271(51):32951-9.
                  pubmed: 8955138doi: 10.1074/jbc.271.51.32951google scholar: lookup
                37. Lascombe MB, Grégoire C, Poncet P, Tavares GA, Rosinski-Chupin I, Rabillon J, Goubran-Botros H, Mazié JC, David B, Alzari PM. Crystal structure of the allergen Equ c 1. A dimeric lipocalin with restricted IgE-reactive epitopes.. J Biol Chem 2000 Jul 14;275(28):21572-7.
                  pubmed: 10787420doi: 10.1074/jbc.m002854200google scholar: lookup
                38. D'Innocenzo B, Salzano AM, D'Ambrosio C, Gazzano A, Niccolini A, Sorce C, Dani FR, Scaloni A, Pelosi P. Secretory proteins as potential semiochemical carriers in the horse.. Biochemistry 2006 Nov 14;45(45):13418-28.
                  pubmed: 17087495doi: 10.1021/bi061409pgoogle scholar: lookup
                39. Montgomery I, Jenkinson DM, Elder HY. The effects of thermal stimulation on the ultrastructure of the fundus and duct of the equine sweat gland.. J Anat 1982 Aug;135(Pt 1):13-28.
                  pmc: PMC1168125pubmed: 7130047
                40. Porter AM. Why do we have apocrine and sebaceous glands?. J R Soc Med 2001 May;94(5):236-7.
                  pmc: PMC1281456pubmed: 11385091doi: 10.1177/014107680109400509google scholar: lookup
                41. Folk GE Jr, Semken HA Jr. The evolution of sweat glands.. Int J Biometeorol 1991 Nov;35(3):180-6.
                  pubmed: 1778649doi: 10.1007/bf01049065google scholar: lookup
                42. Cooper A, Kennedy MW, Fleming RI, Wilson EH, Videler H, Wokosin DL, Su TJ, Green RJ, Lu JR. Adsorption of frog foam nest proteins at the air-water interface.. Biophys J 2005 Mar;88(3):2114-25.
                  pmc: PMC1305263pubmed: 15626715doi: 10.1529/biophysj.104.046268google scholar: lookup
                43. Fleming RI, Mackenzie CD, Cooper A, Kennedy MW. Foam nest components of the túngara frog: a cocktail of proteins conferring physical and biological resilience.. Proc Biol Sci 2009 May 22;276(1663):1787-95.
                  pmc: PMC2674504pubmed: 19324764doi: 10.1098/rspb.2008.1939google scholar: lookup
                44. Sreerama N, Woody RW. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set.. Anal Biochem 2000 Dec 15;287(2):252-60.
                  pubmed: 11112271doi: 10.1006/abio.2000.4880google scholar: lookup
                45. Sreerama N, Woody RW. A self-consistent method for the analysis of protein secondary structure from circular dichroism.. Anal Biochem 1993 Feb 15;209(1):32-44.
                  pubmed: 8465960doi: 10.1006/abio.1993.1079google scholar: lookup
                46. Lu JR, Zhao XB, Yaseen M. Protein adsorption studied by neutron reflection.. Current Opinion in Colloid & Interface Science 2007;12:9–16.
                47. Lu JR, Su TJ, Penfold J. Adsorption of serum albumins at the air/water interface.. Langmuir 1999;15:6975–6983.
                48. Lu JR, Su TJ, Thomas RK. Structural Conformation of Bovine Serum Albumin Layers at the Air-Water Interface Studied by Neutron Reflection.. J Colloid Interface Sci 1999 May 15;213(2):426-437.
                  pubmed: 10222084doi: 10.1006/jcis.1999.6157google scholar: lookup
                49. Lu JR, Su TJ, Thomas RK, Penfold J, Webster J. Structural conformation of lysozyme layers at the air/water interface studied by neutron reflection.. Journal of the Chemical Society-Faraday Transactions 1998;94:3279–3287.
                50. Lu JR, Thomas RK. Neutron reflection from wet interfaces.. Journal of the Chemical Society-Faraday Transactions 1998;94:995–1018.
                51. Lu JR, Thomas RK, Penfold J. Surfactant layers at the air/water interface: structure and composition.. Adv Colloid Interface Sci 2000 Jan 1;84(1-3):143-304.
                  pubmed: 10696453doi: 10.1016/s0001-8686(99)00019-6google scholar: lookup
                52. Dayhoff MO, Schwartz RM, Orcutt BC, editors. Atlas of Protein and Sequence Structure. Washington D.C.: National Biomedical Research Foundation; 1979.
                53. Henikoff S, Henikoff JG. Amino acid substitution matrices from protein blocks.. Proc Natl Acad Sci U S A 1992 Nov 15;89(22):10915-9.
                  pmc: PMC50453pubmed: 1438297doi: 10.1073/pnas.89.22.10915google scholar: lookup

                Citations

                This article has been cited 33 times.
                1. Zahradnik E, Sander I, Lotz A, Liebers V, Thullner I, Tacke S, Raulf M. Exposure levels of animal allergens, endotoxin, and β-(1,3)-glucan on a university campus of veterinary medicine. PLoS One 2023;18(7):e0288522.
                  doi: 10.1371/journal.pone.0288522pubmed: 37440536google scholar: lookup
                2. Brownlow M, Mizzi JX. An Overview of Exertional Heat Illness in Thoroughbred Racehorses: Pathophysiology, Diagnosis, and Treatment Rationale. Animals (Basel) 2023 Feb 9;13(4).
                  doi: 10.3390/ani13040610pubmed: 36830397google scholar: lookup
                3. Senra RL, Ramírez-López CJ, Magalhães-Júnior MJ, Neves JGDS, Barros E, Waddington B, Guimarães SEF, Guimarães JD, Baracat-Pereira MC. Kallikrein proteoforms and reproductive parameters in stallion are conditioned by climate. Sci Rep 2022 Nov 4;12(1):18690.
                  doi: 10.1038/s41598-022-21350-wpubmed: 36333376google scholar: lookup
                4. Patterson Rosa L, Mallicote MF, MacKay RJ, Brooks SA. Ion Channel and Ubiquitin Differential Expression during Erythromycin-Induced Anhidrosis in Foals. Animals (Basel) 2021 Nov 25;11(12).
                  doi: 10.3390/ani11123379pubmed: 34944156google scholar: lookup
                5. Kang H, Zsoldos RR, Woldeyohannes SM, Gaughan JB, Sole Guitart A. The Use of Percutaneous Thermal Sensing Microchips for Body Temperature Measurements in Horses Prior to, during and after Treadmill Exercise. Animals (Basel) 2020 Dec 2;10(12).
                  doi: 10.3390/ani10122274pubmed: 33276500google scholar: lookup
                6. Nandula SR, Huxford I, Wheeler TT, Aparicio C, Gorr SU. The parotid secretory protein BPIFA2 is a salivary surfactant that affects lipopolysaccharide action. Exp Physiol 2020 Aug;105(8):1280-1292.
                  doi: 10.1113/EP088567pubmed: 32390232google scholar: lookup
                7. Al Abri MA, Holl HM, Kalla SE, Sutter NB, Brooks SA. Whole genome detection of sequence and structural polymorphism in six diverse horses. PLoS One 2020;15(4):e0230899.
                  doi: 10.1371/journal.pone.0230899pubmed: 32271776google scholar: lookup
                8. Zhang H, Burrows J, Card GL, Attwood G, Wheeler TT, Arcus VL. The three dimensional structure of Bovine Salivary Protein 30b (BSP30b) and its interaction with specific rumen bacteria. PLoS One 2019;14(4):e0206709.
                  doi: 10.1371/journal.pone.0206709pubmed: 30978191google scholar: lookup
                9. Kamus L, Rameau M, Theoret C. Feasibility of a disposable canister-free negative-pressure wound therapy (NPWT) device for treating open wounds in horses. BMC Vet Res 2019 Mar 6;15(1):78.
                  doi: 10.1186/s12917-019-1829-5pubmed: 30841889google scholar: lookup
                10. Jappe U, Schwager C, Schromm AB, González Roldán N, Stein K, Heine H, Duda KA. Lipophilic Allergens, Different Modes of Allergen-Lipid Interaction and Their Impact on Asthma and Allergy. Front Immunol 2019;10:122.
                  doi: 10.3389/fimmu.2019.00122pubmed: 30837983google scholar: lookup
                11. Victor S, Binnmyr J, Lampa E, Rask-Andersen A, Elfman L. Levels of horse allergen Equ c 4 in dander and saliva from ten horse breeds. Clin Exp Allergy 2019 May;49(5):701-711.
                  doi: 10.1111/cea.13362pubmed: 30716182google scholar: lookup
                12. Curin M, Hilger C. Allergy to pets and new allergies to uncommon pets. Allergol Select 2017;1(2):214-221.
                  doi: 10.5414/ALX01842Epubmed: 30402618google scholar: lookup
                13. Cooper A, Vance SJ, Smith BO, Kennedy MW. Frog foams and natural protein surfactants. Colloids Surf A Physicochem Eng Asp 2017 Dec 5;534:120-129.
                  doi: 10.1016/j.colsurfa.2017.01.049pubmed: 29276339google scholar: lookup
                14. Zahradnik E, Raulf M. Respiratory Allergens from Furred Mammals: Environmental and Occupational Exposure. Vet Sci 2017 Aug 4;4(3).
                  doi: 10.3390/vetsci4030038pubmed: 29056697google scholar: lookup
                15. Hilger C, van Hage M, Kuehn A. Diagnosis of Allergy to Mammals and Fish: Cross-Reactive vs. Specific Markers. Curr Allergy Asthma Rep 2017 Aug 22;17(9):64.
                  doi: 10.1007/s11882-017-0732-zpubmed: 28831729google scholar: lookup
                16. Wong LH, Levine TP. Tubular lipid binding proteins (TULIPs) growing everywhere. Biochim Biophys Acta Mol Cell Res 2017 Sep;1864(9):1439-1449.
                  doi: 10.1016/j.bbamcr.2017.05.019pubmed: 28554774google scholar: lookup
                17. Morris RJ, Brandani GB, Desai V, Smith BO, Schor M, MacPhee CE. The Conformation of Interfacially Adsorbed Ranaspumin-2 Is an Arrested State on the Unfolding Pathway. Biophys J 2016 Aug 23;111(4):732-742.
                  doi: 10.1016/j.bpj.2016.06.006pubmed: 27558717google scholar: lookup
                18. Schor M, Reid JL, MacPhee CE, Stanley-Wall NR. The Diverse Structures and Functions of Surfactant Proteins. Trends Biochem Sci 2016 Jul;41(7):610-620.
                  doi: 10.1016/j.tibs.2016.04.009pubmed: 27242193google scholar: lookup
                19. Vance SJ, Desai V, Smith BO, Kennedy MW, Cooper A. Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2. Biophys Chem 2016 Jul-Aug;214-215:27-32.
                  doi: 10.1016/j.bpc.2016.05.003pubmed: 27214760google scholar: lookup
                20. Walton WG, Ahmad S, Little MS, Kim CS, Tyrrell J, Lin Q, Di YP, Tarran R, Redinbo MR. Structural Features Essential to the Antimicrobial Functions of Human SPLUNC1. Biochemistry 2016 May 31;55(21):2979-91.
                  doi: 10.1021/acs.biochem.6b00271pubmed: 27145151google scholar: lookup
                21. Vance SJ, McDonald RE, Cooper A, Smith BO, Kennedy MW. The structure of latherin, a surfactant allergen protein from horse sweat and saliva. J R Soc Interface 2013 Aug 6;10(85):20130453.
                  doi: 10.1098/rsif.2013.0453pubmed: 23782536google scholar: lookup
                22. Vance SJ, McDonald RE, Cooper A, Kennedy MW, Smith BO. Resonance assignments for latherin, a natural surfactant protein from horse sweat. Biomol NMR Assign 2014 Apr;8(1):213-6.
                  doi: 10.1007/s12104-013-9485-3pubmed: 23708874google scholar: lookup
                23. Abdolhosseini M, Nandula SR, Song J, Hirt H, Gorr SU. Lysine substitutions convert a bacterial-agglutinating peptide into a bactericidal peptide that retains anti-lipopolysaccharide activity and low hemolytic activity. Peptides 2012 Jun;35(2):231-8.
                  doi: 10.1016/j.peptides.2012.03.017pubmed: 22484285google scholar: lookup
                24. Gorr SU. Antimicrobial peptides in periodontal innate defense. Front Oral Biol 2012;15:84-98.
                  doi: 10.1159/000329673pubmed: 22142958google scholar: lookup
                25. Gorr SU, Abdolhosseini M, Shelar A, Sotsky J. Dual host-defence functions of SPLUNC2/PSP and synthetic peptides derived from the protein. Biochem Soc Trans 2011 Aug;39(4):1028-32.
                  doi: 10.1042/BST0391028pubmed: 21787342google scholar: lookup
                26. Bartlett JA, Gakhar L, Penterman J, Singh PK, Mallampalli RK, Porter E, McCray PB Jr. PLUNC: a multifunctional surfactant of the airways. Biochem Soc Trans 2011 Aug;39(4):1012-6.
                  doi: 10.1042/BST0391012pubmed: 21787339google scholar: lookup
                27. Bingle CD, Seal RL, Craven CJ. Systematic nomenclature for the PLUNC/PSP/BSP30/SMGB proteins as a subfamily of the BPI fold-containing superfamily. Biochem Soc Trans 2011 Aug;39(4):977-83.
                  doi: 10.1042/BST0390977pubmed: 21787333google scholar: lookup
                28. Chiang SC, Veldhuizen EJ, Barnes FA, Craven CJ, Haagsman HP, Bingle CD. Identification and characterisation of the BPI/LBP/PLUNC-like gene repertoire in chickens reveals the absence of a LBP gene. Dev Comp Immunol 2011 Mar;35(3):285-95.
                  doi: 10.1016/j.dci.2010.09.013pubmed: 20959152google scholar: lookup
                29. McGillivary G, Bakaletz LO. The multifunctional host defense peptide SPLUNC1 is critical for homeostasis of the mammalian upper airway. PLoS One 2010 Oct 7;5(10):e13224.
                  doi: 10.1371/journal.pone.0013224pubmed: 20949060google scholar: lookup
                30. Cooper A, Kennedy MW. Biofoams and natural protein surfactants. Biophys Chem 2010 Oct;151(3):96-104.
                  doi: 10.1016/j.bpc.2010.06.006pubmed: 20615601google scholar: lookup
                31. Gakhar L, Bartlett JA, Penterman J, Mizrachi D, Singh PK, Mallampalli RK, Ramaswamy S, McCray PB Jr. PLUNC is a novel airway surfactant protein with anti-biofilm activity. PLoS One 2010 Feb 9;5(2):e9098.
                  doi: 10.1371/journal.pone.0009098pubmed: 20161732google scholar: lookup
                32. Rosada T, Lis K, Bartuzi Z, Ukleja-Sokołowska N. Sensitization to Horse Allergens-Molecular Analysis Based on the Results of Multiparameter Tests. Int J Mol Sci 2025 Feb 9;26(4).
                  doi: 10.3390/ijms26041447pubmed: 40003913google scholar: lookup
                33. Retzinger AC, Retzinger GS. The Acari Hypothesis, V: deciphering allergenicity. Front Allergy 2024;5:1454292.
                  doi: 10.3389/falgy.2024.1454292pubmed: 39552700google scholar: lookup
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