FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / PLoS One / Development of ELISA based on Bacillus anthracis capsule bio...
PloS one2021; 16(10); e0258317; doi: 10.1371/journal.pone.0258317

Development of ELISA based on Bacillus anthracis capsule biosynthesis protein CapA for naturally acquired antibodies against anthrax.

Abstract: Anthrax is a zoonotic disease caused by the gram-positive spore-forming bacterium Bacillus anthracis. Detecting naturally acquired antibodies against anthrax sublethal exposure in animals is essential for anthrax surveillance and effective control measures. Serological assays based on protective antigen (PA) of B. anthracis are mainly used for anthrax surveillance and vaccine evaluation. Although the assay is reliable, it is challenging to distinguish the naturally acquired antibodies from vaccine-induced immunity in animals because PA is cross-reactive to both antibodies. Although additional data on the vaccination history of animals could bypass this problem, such data are not readily accessible in many cases. In this study, we established a new enzyme-linked immunosorbent assay (ELISA) specific to antibodies against capsule biosynthesis protein CapA antigen of B. anthracis, which is non-cross-reactive to vaccine-induced antibodies in horses. Using in silico analyses, we screened coding sequences encoded on pXO2 plasmid, which is absent in the veterinary vaccine strain Sterne 34F2 but present in virulent strains of B. anthracis. Among the 8 selected antigen candidates, capsule biosynthesis protein CapA (GBAA_RS28240) and peptide ABC transporter substrate-binding protein (GBAA_RS28340) were detected by antibodies in infected horse sera. Of these, CapA has not yet been identified as immunoreactive in other studies to the best of our knowledge. Considering the protein solubility and specificity of B. anthracis, we prepared the C-terminus region of CapA, named CapA322, and developed CapA322-ELISA based on a horse model. Comparative analysis of the CapA322-ELISA and PAD1-ELISA (ELISA uses domain one of the PA) showed that CapA322-ELISA could detect anti-CapA antibodies in sera from infected horses but was non-reactive to sera from vaccinated horses. The CapA322-ELISA could contribute to the anthrax surveillance in endemic areas, and two immunoreactive proteins identified in this study could be additives to the improvement of current or future vaccine development.
Get Full Text
Publication Date: 2021-10-11 PubMed ID: 34634075PubMed Central: PMC8504768DOI: 10.1371/journal.pone.0258317Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

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 study discusses the development of an Enzyme-Linked Immunosorbent Assay (ELISA) method that is specific for identifying naturally acquired anthrax antibodies in animals. Instead of relying on the commonly used protective antigen (PA) which can lead to confusion between natural and vaccine-acquired immunity, this ELISA method uses the CapA from Bacillus anthracis, a protein distinct from what’s included in existing vaccines.

Development of the CapA322-ELISA

  • The need for a new ELISA method arose due to the difficulty in differentiating natural immunity against anthrax from vaccinated immunity in animals using the existing methods which primarily rely on the protective antigen (PA).
  • The authors initially screened the pXO2 plasmid, a sequence not present in the common veterinary vaccine but found in virulent B. anthracis strains, using in silico analyses.
  • Out of 8 antigen candidates, they found that capsule biosynthesis protein CapA and peptide ABC transporter substrate-binding protein could be detected by antibodies present in the sera of infected horses.
  • Among these, CapA was unique because it had not been previously identified as immunoreactive. They prepared the C-terminus region of CapA, named CapA322, and developed CapA322-ELISA.

Comparison and Results of CapA322-ELISA

  • The authors then compared the performance of CapA322-ELISA with PAD1-ELISA which relies on the PA’s domain one.
  • Results showed that CapA322-ELISA was able to detect anti-CapA antibodies from sera of infected horses but had no reaction to sera from vaccinated horses. This differentiated it from PAD1-ELISA which is cross-reactive to both antibodies.

Implications and Future Work

  • CapA322-ELISA could be an effective tool in anthrax surveillance specifically in areas where the disease is endemic.
  • In addition, the newly identified immunoreactive proteins may be useful in enhancing existing or developing new vaccines.
  • However, since this study only used horse sera, further research might be needed to test its applicability to other animals.

Cite This Article

APA
Zorigt T, Furuta Y, Simbotwe M, Ochi A, Tsujinouchi M, Shawa M, Shimizu T, Isoda N, Enkhtuya J, Higashi H. (2021). Development of ELISA based on Bacillus anthracis capsule biosynthesis protein CapA for naturally acquired antibodies against anthrax. PLoS One, 16(10), e0258317. https://doi.org/10.1371/journal.pone.0258317

Publication

PloS one
ISSN: 1932-6203
NlmUniqueID: 101285081
Country: United States
Language: English
Volume: 16
Issue: 10
Pages: e0258317

Researcher Affiliations

Zorigt, Tuvshinzaya
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
  • Graduate School of Infectious Diseases, School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Furuta, Yoshikazu
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
  • Graduate School of Infectious Diseases, School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Simbotwe, Manyando
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
Ochi, Akihiro
  • Equine Research Institute, Japan Racing Association, Shimotsuke, Tochigi, Japan.
Tsujinouchi, Mai
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
Shawa, Misheck
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
  • Graduate School of Infectious Diseases, School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Shimizu, Tomoko
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
Isoda, Norikazu
  • Laboratory of Microbiology, School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Enkhtuya, Jargalsaikhan
  • Laboratory of Food Hygiene, Institute of Veterinary Medicine, Ulaanbaatar, Mongolia.
Higashi, Hideaki
  • Division of Infection and Immunity, International Institute for Zoonosis Control (Former Research Center for Zoonosis Control), Hokkaido University, Sapporo, Japan.
  • Graduate School of Infectious Diseases, School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.

MeSH Terms

  • Animals
  • Anthrax / immunology
  • Anthrax Vaccines / immunology
  • Antibodies, Bacterial / immunology
  • Antigens, Bacterial / immunology
  • Bacillus anthracis / immunology
  • Bacterial Capsules / immunology
  • Bacterial Proteins / immunology
  • Bacterial Proteins / isolation & purification
  • Enzyme-Linked Immunosorbent Assay / methods
  • Heat-Shock Proteins / immunology
  • Heat-Shock Proteins / isolation & purification
  • Horses
  • Immunoglobulin G / immunology
  • Plasmids / metabolism
  • Sequence Homology, Amino Acid
  • Spores, Bacterial / immunology

Conflict of Interest Statement

The authors have declared that no competing interests exist.

References

This article includes 71 references
  1. Carlson CJ, Kracalik IT, Ross N, Alexander KA, Hugh-Jones ME, Fegan M. The global distribution of Bacillus anthracis and associated anthrax risk to humans, livestock and wildlife.. .
    pubmed: 31086311
  2. Sitali DC, Twambo MC, Chisoni M, Bwalya MJ, Munyeme M. Lay perceptions, beliefs and practices linked to the persistence of anthrax outbreaks in cattle in the Western Province of Zambia.. Onderstepoort J Vet Res 2018;85(1):e1–e8.
    doi: 10.4102/ojvr.v85i1.1615pmc: PMC6238791pubmed: 30198281google scholar: lookup
  3. Driciru M, Rwego IB, Asiimwe B, Travis DA, Alvarez J, VanderWaal K. Spatio-temporal epidemiology of anthrax in Hippopotamus amphibious in Queen Elizabeth Protected Area, Uganda.. PLoS One 2018;13(11):e0206922.
    doi: 10.1371/journal.pone.0206922pmc: PMC6261556pubmed: 30485342google scholar: lookup
  4. Kanankege KST, Abdrakhmanov SK, Alvarez J, Glaser L, Bender JB, Mukhanbetkaliyev YY. Comparison of spatiotemporal patterns of historic natural Anthrax outbreaks in Minnesota and Kazakhstan.. PLoS One 2019;14(5):e0217144.
    doi: 10.1371/journal.pone.0217144pmc: PMC6524940pubmed: 31100100google scholar: lookup
  5. Chen WJ, Lai SJ, Yang Y, Liu K, Li XL, Yao HW. Mapping the Distribution of Anthrax in Mainland China, 2005–2013.. PLoS Negl Trop Dis 2016;10(4):e0004637.
    doi: 10.1371/journal.pntd.0004637pmc: PMC4838246pubmed: 27097318google scholar: lookup
  6. Vieira AR, Salzer JS, Traxler RM, Hendricks KA, Kadzik ME, Marston CK. Enhancing Surveillance and Diagnostics in Anthrax-Endemic Countries.. Emerg Infect Dis 2017;23(13):S147–53.
    doi: 10.3201/eid2313.170431pmc: PMC5711320pubmed: 29155651google scholar: lookup
  7. Okutani A, Tungalag H, Boldbaatar B, Yamada A, Tserennorov D, Otgonchimeg I. Molecular epidemiological study of Bacillus anthracis isolated in Mongolia by multiple-locus variable-number tandem-repeat analysis for 8 loci (MLVA-8).. Jpn J Infect Dis 2011;64(4):345–8.
    pubmed: 21788715
  8. Mock M, Fouet A. Anthrax.. Annual Review of Microbiology 2001;55(1):647–71.
    doi: 10.1146/annurev.micro.55.1.647pubmed: 11544370google scholar: lookup
  9. Hugh-Jones ME, de Vos V. Anthrax and wildlife.. Rev Sci Tech 2002;21(2):359–83.
    doi: 10.20506/rst.21.2.1336pubmed: 11974621google scholar: lookup
  10. Ganeva D. ANALYSIS OF THE BULGARIAN TABANID FAUNA WITH REGARD TO ITS POTENTIAL FOR EPIDEMIOLOGICAL INVOLVEMENT D. J. GANEVA.. Bulgarian Journal of Veterinary Medicine 2004;7(1):1–8.
  11. Turell MJ, Knudson GB. Mechanical transmission of Bacillus anthracis by stable flies (Stomoxys calcitrans) and mosquitoes (Aedes aegypti and Aedes taeniorhynchus).. Infect Immun 1987;55(8):1859–61.
    doi: 10.1128/iai.55.8.1859-1861.1987pmc: PMC260614pubmed: 3112013google scholar: lookup
  12. WHO Guidelines Approved by the Guidelines Review Committee. Anthrax in Humans and Animals.. World Health Organization 2008.
  13. Mogridge J, Cunningham K, Collier RJ. Stoichiometry of anthrax toxin complexes.. Biochemistry 2002;41(3):1079–82.
    doi: 10.1021/bi015860mpubmed: 11790132google scholar: lookup
  14. Leppla SH. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells.. Proc Natl Acad Sci U S A 1982;79(10):3162–6.
    doi: 10.1073/pnas.79.10.3162pmc: PMC346374pubmed: 6285339google scholar: lookup
  15. Duesbery NS, Webb CP, Leppla SH, Gordon VM, Klimpel KR, Copeland TD. Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor.. Science 1998;280(5364):734–7.
    doi: 10.1126/science.280.5364.734pubmed: 9563949google scholar: lookup
  16. Drysdale M, Heninger S, Hutt J, Chen Y, Lyons CR, Koehler TM. Capsule synthesis by Bacillus anthracis is required for dissemination in murine inhalation anthrax.. Embo j 2005;24(1):221–7.
    doi: 10.1038/sj.emboj.7600495pmc: PMC544908pubmed: 15616593google scholar: lookup
  17. Jelacic TM, Chabot DJ, Bozue JA, Tobery SA, West MW, Moody K. Exposure to Bacillus anthracis capsule results in suppression of human monocyte-derived dendritic cells.. Infect Immun 2014;82(8):3405–16.
    doi: 10.1128/IAI.01857-14pmc: PMC4136234pubmed: 24891109google scholar: lookup
  18. Glinert I, Weiss S, Sittner A, Bar-David E, Ben-Shmuel A, Schlomovitz J. Infection with a Nonencapsulated Bacillus anthracis Strain in Rabbits-The Role of Bacterial Adhesion and the Potential for a Safe Live Attenuated Vaccine.. Toxins (Basel) 2018;10(12).
    doi: 10.3390/toxins10120506pmc: PMC6316610pubmed: 30513757google scholar: lookup
  19. Turnbull PC. Anthrax vaccines: past, present and future.. Vaccine 1991;9(8):533–9.
    doi: 10.1016/0264-410x(91)90237-zpubmed: 1771966google scholar: lookup
  20. Turnbull PC, Doganay M, Lindeque PM, Aygen B, McLaughlin J. Serology and anthrax in humans, livestock and Etosha National Park wildlife.. Epidemiol Infect 1992;108(2):299–313.
    doi: 10.1017/s0950268800049773pmc: PMC2271992pubmed: 1582472google scholar: lookup
  21. Hampson K, Lembo T, Bessell P, Auty H, Packer C, Halliday J. Predictability of anthrax infection in the Serengeti, Tanzania.. J Appl Ecol 2011;48(6):1333–44.
    doi: 10.1111/j.1365-2664.2011.02030.xpmc: PMC3272456pubmed: 22318563google scholar: lookup
  22. Lembo T, Hampson K, Auty H, Beesley CA, Bessell P, Packer C. Serologic surveillance of anthrax in the Serengeti ecosystem, Tanzania, 1996–2009.. Emerg Infect Dis 2011;17(3):387–94.
    doi: 10.3201/eid1703.101290pmc: PMC3166018pubmed: 21392428google scholar: lookup
  23. Reuveny S, White MD, Adar YY, Kafri Y, Altboum Z, Gozes Y. Search for correlates of protective immunity conferred by anthrax vaccine.. Infect Immun 2001;69(5):2888–93.
    doi: 10.1128/IAI.69.5.2888-2893.2001pmc: PMC98239pubmed: 11292703google scholar: lookup
  24. Marcus H, Danieli R, Epstein E, Velan B, Shafferman A, Reuveny S. Contribution of immunological memory to protective immunity conferred by a Bacillus anthracis protective antigen-based vaccine.. Infect Immun 2004;72(6):3471–7.
    doi: 10.1128/IAI.72.6.3471-3477.2004pmc: PMC415724pubmed: 15155654google scholar: lookup
  25. Stear M. OIE Manual of Diagnostic Tests and Vaccines for Terrestrial Animals (Mammals, Birds and Bees) 5th Edn. Volumes 1 & 2.. Parasitology 2005;130:727–.
    doi: 10.1017/S0031182005007699google scholar: lookup
  26. Beyer W, Glöckner P, Otto J, Böhm R. A nested PCR method for the detection of Bacillus anthracis in environmental samples collected from former tannery sites.. Microbiological Research 1995;150(2):179–86.
    doi: 10.1016/S0944-5013(11)80054-6pubmed: 7600011google scholar: lookup
  27. Simbotwe M, Fujikura D, Ohnuma M, Omori R, Furuta Y, Muuka GM. Correction: Development and application of a Bacillus anthracis protective antigen domain-1 in-house ELISA for the detection of anti-protective antigen antibodies in cattle in Zambia.. PLoS One 2019;p. e0211592.
    doi: 10.1371/journal.pone.0211592pmc: PMC6347153pubmed: 30682188google scholar: lookup
  28. Nakai K, Horton P. PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization.. Trends Biochem Sci 1999;24(1):34–6.
    doi: 10.1016/s0968-0004(98)01336-xpubmed: 10087920google scholar: lookup
  29. Emanuelsson O, Brunak S, von Heijne G, Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools.. Nat Protoc 2007;2(4):953–71.
    doi: 10.1038/nprot.2007.131pubmed: 17446895google scholar: lookup
  30. Juncker AS, Willenbrock H, Von Heijne G, Brunak S, Nielsen H, Krogh A. Prediction of lipoprotein signal peptides in Gram-negative bacteria.. Protein Sci 2003;12(8):1652–62.
    doi: 10.1110/ps.0303703pmc: PMC2323952pubmed: 12876315google scholar: lookup
  31. Krogh A, Larsson B, von Heijne G, Sonnhammer EL. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes.. J Mol Biol 2001;305(3):567–80.
    doi: 10.1006/jmbi.2000.4315pubmed: 11152613google scholar: lookup
  32. Hulo N, Bairoch A, Bulliard V, Cerutti L, Cuche BA, de Castro E. The 20 years of PROSITE.. Nucleic Acids Res 2008;36(Database issue):D245-9.
    doi: 10.1093/nar/gkm977pmc: PMC2238851pubmed: 18003654google scholar: lookup
  33. Ohnishi N, Maruyama F, Ogawa H, Kachi H, Yamada S, Fujikura D. Genome Sequence of a Bacillus anthracis Outbreak Strain from Zambia, 2011.. Genome Announc 2014;2(2).
    doi: 10.1128/genomeA.00116-14pmc: PMC3945500pubmed: 24604644google scholar: lookup
  34. Gibson DG, Young L, Chuang RY, Venter JC, Hutchison CA 3rd, Smith HO. Enzymatic assembly of DNA molecules up to several hundred kilobases.. Nat Methods 2009;6(5):343–5.
    doi: 10.1038/nmeth.1318pubmed: 19363495google scholar: lookup
  35. Crowther JR. The ELISA guidebook.. Methods Mol Biol 2000;149:Iii-iv, 1–413.
    doi: 10.1385/1592590497pubmed: 11028258google scholar: lookup
  36. Ariel N, Zvi A, Grosfeld H, Gat O, Inbar Y, Velan B. Search for potential vaccine candidate open reading frames in the Bacillus anthracis virulence plasmid pXO1: in silico and in vitro screening.. Infect Immun 2002;70(12):6817–27.
    doi: 10.1128/IAI.70.12.6817-6827.2002pmc: PMC133087pubmed: 12438358google scholar: lookup
  37. María RA, Castelán J, Alicia J, Monterrubio G, Gerardo A. The Impact of Bioinformatics on Vaccine Design and Development.. 2017.
  38. Smith DB, Johnson KS. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase.. Gene 1988;67(1):31–40.
    doi: 10.1016/0378-1119(88)90005-4pubmed: 3047011google scholar: lookup
  39. Jeong H, Kim HJ, Lee SJ. Complete Genome Sequence of Escherichia coli Strain BL21.. Genome Announc 2015;3(2).
    doi: 10.1128/genomeA.00134-15pmc: PMC4395058pubmed: 25792055google scholar: lookup
  40. Carlson CJ, Getz WM, Kausrud KL, Cizauskas CA, Blackburn JK, Bustos Carrillo FA. Spores and soil from six sides: interdisciplinarity and the environmental biology of anthrax (Bacillus anthracis).. Biol Rev Camb Philos Soc 2018;93(4):1813–31.
    doi: 10.1111/brv.12420pubmed: 29732670google scholar: lookup
  41. Candela T, Fouet A. Bacillus anthracis CapD, belonging to the gamma-glutamyltranspeptidase family, is required for the covalent anchoring of capsule to peptidoglycan.. Mol Microbiol 2005;57(3):717–26.
    doi: 10.1111/j.1365-2958.2005.04718.xpubmed: 16045616google scholar: lookup
  42. Lu S, Wang J, Chitsaz F, Derbyshire MK, Geer RC, Gonzales NR. CDD/SPARCLE: the conserved domain database in 2020.. Nucleic Acids Res 2020;48(D1):D265–d8.
    doi: 10.1093/nar/gkz991pmc: PMC6943070pubmed: 31777944google scholar: lookup
  43. Pizza M, Scarlato V, Masignani V, Giuliani MM, Aricò B, Comanducci M. Identification of vaccine candidates against serogroup B meningococcus by whole-genome sequencing.. Science 2000;287(5459):1816–20.
    doi: 10.1126/science.287.5459.1816pubmed: 10710308google scholar: lookup
  44. Sutcliffe IC, Harrington DJ. Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes.. Microbiology (Reading) 2002;148(Pt 7):2065–77.
    doi: 10.1099/00221287-148-7-2065pubmed: 12101295google scholar: lookup
  45. Chakravarti DN, Fiske MJ, Fletcher LD, Zagursky RJ. Application of genomics and proteomics for identification of bacterial gene products as potential vaccine candidates.. Vaccine 2000;19(6):601–12.
    doi: 10.1016/s0264-410x(00)00256-5pubmed: 11090710google scholar: lookup
  46. Chaudhuri R, Kulshreshtha D, Raghunandanan MV, Ramachandran S. Integrative immunoinformatics for Mycobacterial diseases in R platform.. Systems and Synthetic Biology 2014;8(1):27–39.
    doi: 10.1007/s11693-014-9135-9pmc: PMC3933634pubmed: 24592289google scholar: lookup
  47. Klee SR, Brzuszkiewicz EB, Nattermann H, Brüggemann H, Dupke S, Wollherr A. The genome of a Bacillus isolate causing anthrax in chimpanzees combines chromosomal properties of B. cereus with B. anthracis virulence plasmids.. PLoS One 2010;5(7):e10986.
    doi: 10.1371/journal.pone.0010986pmc: PMC2901330pubmed: 20634886google scholar: lookup
  48. Hoffmaster AR, Hill KK, Gee JE, Marston CK, De BK, Popovic T. Characterization of Bacillus cereus isolates associated with fatal pneumonias: strains are closely related to Bacillus anthracis and harbor B. anthracis virulence genes.. J Clin Microbiol 2006;44(9):3352–60.
    doi: 10.1128/JCM.00561-06pmc: PMC1594744pubmed: 16954272google scholar: lookup
  49. Baldwin VM. You Can’t B. cereus–A Review of Bacillus cereus Strains That Cause Anthrax-Like Disease.. Frontiers in Microbiology 2020;11:1731.
    doi: 10.3389/fmicb.2020.01731pmc: PMC7468541pubmed: 32973690google scholar: lookup
  50. Han CS, Xie G, Challacombe JF, Altherr MR, Bhotika SS, Brown N. Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis.. J Bacteriol 2006;188(9):3382–90.
    doi: 10.1128/JB.188.9.3382-3390.2006pmc: PMC1447445pubmed: 16621833google scholar: lookup
  51. Sergeev N, Distler M, Vargas M, Chizhikov V, Herold KE, Rasooly A. Microarray analysis of Bacillus cereus group virulence factors.. J Microbiol Methods 2006;65(3):488–502.
    doi: 10.1016/j.mimet.2005.09.013pubmed: 16242802google scholar: lookup
  52. Cachat E, Barker M, Read TD, Priest FG. A Bacillus thuringiensis strain producing a polyglutamate capsule resembling that of Bacillus anthracis.. FEMS Microbiol Lett 2008;285(2):220–6.
    doi: 10.1111/j.1574-6968.2008.01231.xpubmed: 18549401google scholar: lookup
  53. Ramisse V, Patra G, Garrigue H, Guesdon JL, Mock M. Identification and characterization of Bacillus anthracis by multiplex PCR analysis of sequences on plasmids pXO1 and pXO2 and chromosomal DNA.. FEMS Microbiol Lett 1996;145(1):9–16.
    doi: 10.1111/j.1574-6968.1996.tb08548.xpubmed: 8931320google scholar: lookup
  54. Kim K, Seo J, Wheeler K, Park C, Kim D, Park S. Rapid genotypic detection of Bacillus anthracis and the Bacillus cereus group by multiplex real-time PCR melting curve analysis.. FEMS Immunol Med Microbiol 2005;43(2):301–10.
    doi: 10.1016/j.femsim.2004.10.005pubmed: 15681162google scholar: lookup
  55. Pannucci J, Okinaka RT, Williams E, Sabin R, Ticknor LO, Kuske CR. DNA sequence conservation between the Bacillus anthracis pXO2 plasmid and genomic sequence from closely related bacteria.. BMC Genomics 2002;3(1):34.
    doi: 10.1186/1471-2164-3-34pmc: PMC140023pubmed: 12473162google scholar: lookup
  56. Ghosh N, Tomar I, Lukka H, Goel AK. Serodiagnosis of Human Cutaneous Anthrax in India Using an Indirect Anti-Lethal Factor IgG Enzyme-Linked Immunosorbent Assay.. Clinical and Vaccine Immunology 2013;20(2):282.
    doi: 10.1128/CVI.00598-12pmc: PMC3571271pubmed: 23269414google scholar: lookup
  57. Ghosh N, Goel AK. Anti-Protective Antigen IgG Enzyme-Linked Immunosorbent Assay for Diagnosis of Cutaneous Anthrax in India.. Clinical and Vaccine Immunology 2012;19(8):1238.
    doi: 10.1128/CVI.00154-12pmc: PMC3416091pubmed: 22718130google scholar: lookup
  58. Harrison LH, Ezzell JW, Abshire TG, Kidd S, Kaufmann AF. Evaluation of serologic tests for diagnosis of anthrax after an outbreak of cutaneous anthrax in Paraguay.. J Infect Dis 1989;160(4):706–10.
    doi: 10.1093/infdis/160.4.706pubmed: 2507648google scholar: lookup
  59. Chen Z, Schneerson R, Lovchik JA, Dai Z, Kubler-Kielb J, Agulto L. Bacillus anthracis Capsular Conjugates Elicit Chimpanzee Polyclonal Antibodies That Protect Mice from Pulmonary Anthrax.. Clin Vaccine Immunol 2015;22(8):902–8.
    doi: 10.1128/CVI.00137-15pmc: PMC4519721pubmed: 26041039google scholar: lookup
  60. Phaswana PH, Ndumnego OC, Koehler SM, Beyer W, Crafford JE, van Heerden H. Use of the mice passive protection test to evaluate the humoral response in goats vaccinated with Sterne 34F2 live spore vaccine.. Vet Res 2017;48(1):46.
    doi: 10.1186/s13567-017-0451-4pmc: PMC5590180pubmed: 28882176google scholar: lookup
  61. McWilliams BD, Palzkill T, Weinstock GM, Petrosino JF. Identification of novel and cross-species seroreactive proteins from Bacillus anthracis using a ligation-independent cloning-based, SOS-inducible expression system.. Microbial Pathogenesis 2012;53(5):250–8.
    doi: 10.1016/j.micpath.2012.08.006pmc: PMC3779308pubmed: 22975444google scholar: lookup
  62. Chitlaru T, Gat O, Grosfeld H, Inbar I, Gozlan Y, Shafferman A. Identification of In Vivo-Expressed Immunogenic Proteins by Serological Proteome Analysis of the Bacillus anthracis Secretome.. Infection and Immunity 2007;75(6):2841.
    doi: 10.1128/IAI.02029-06pmc: PMC1932864pubmed: 17353282google scholar: lookup
  63. Gat O, Grosfeld H, Ariel N, Inbar I, Zaide G, Broder Y. Search for Bacillus anthracis potential vaccine candidates by a functional genomic-serologic screen.. Infect Immun 2006;74(7):3987–4001.
    doi: 10.1128/IAI.00174-06pmc: PMC1489694pubmed: 16790772google scholar: lookup
  64. Kempsell KE, Kidd SP, Lewandowski K, Elmore MJ, Charlton S, Yeates A. Whole genome protein microarrays for serum profiling of immunodominant antigens of Bacillus anthracis.. Front Microbiol 2015;6:747.
    doi: 10.3389/fmicb.2015.00747pmc: PMC4534840pubmed: 26322022google scholar: lookup
  65. Turnbull PC, Broster MG, Carman JA, Manchee RJ, Melling J. Development of antibodies to protective antigen and lethal factor components of anthrax toxin in humans and guinea pigs and their relevance to protective immunity.. Infect Immun 1986;52(2):356–63.
    doi: 10.1128/iai.52.2.356-363.1986pmc: PMC261006pubmed: 3084381google scholar: lookup
  66. Grabenstein JD. Vaccines: countering anthrax: vaccines and immunoglobulins.. Clin Infect Dis 2008;46(1):129–36.
    doi: 10.1086/523578pubmed: 18171228google scholar: lookup
  67. Ivins BE, Welkos SL, Little SF, Crumrine MH, Nelson GO. Immunization against anthrax with Bacillus anthracis protective antigen combined with adjuvants.. Infect Immun 1992;60(2):662–8.
    doi: 10.1128/iai.60.2.662-668.1992pmc: PMC257681pubmed: 1730501google scholar: lookup
  68. Ivins B, Fellows P, Pitt L, Estep J, Farchaus J, Friedlander A. Experimental anthrax vaccines: efficacy of adjuvants combined with protective antigen against an aerosol Bacillus anthracis spore challenge in guinea pigs.. Vaccine 1995;13(18):1779–84.
    doi: 10.1016/0264-410x(95)00139-rpubmed: 8701593google scholar: lookup
  69. Ivins BE, Pitt ML, Fellows PF, Farchaus JW, Benner GE, Waag DM. Comparative efficacy of experimental anthrax vaccine candidates against inhalation anthrax in rhesus macaques.. Vaccine 1998;16(11–12):1141–8.
    doi: 10.1016/s0264-410x(98)80112-6pubmed: 9682372google scholar: lookup
  70. Welkos SL, Friedlander AM. Comparative safety and efficacy against Bacillus anthracis of protective antigen and live vaccines in mice.. Microb Pathog 1988;5(2):127–39.
    doi: 10.1016/0882-4010(88)90015-0pubmed: 3148815google scholar: lookup
  71. Jefferson T, Rudin M, DiPietrantonj C. Systematic review of the effects of pertussis vaccines in children.. Vaccine 2003;21(17–18):2003–14.
    doi: 10.1016/s0264-410x(02)00770-3pubmed: 12706690google scholar: lookup

Citations

This article has been cited 0 times.
Subscribe to our newsletter
Join 99,002 horse owners like you who receive our email updates on horse health and nutrition.