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Identification of a novel collagen-like protein, SclC, in Streptococcus equi using signal sequence phage display.
Abstract: Strangles is a serious disease in horses caused by Streptococcus equi subspecies equi. In this study, genes encoding putative extracellular proteins in this subspecies have been identified using signal sequence phage display. Among these, one showed similarities to the SclB protein, a member of the collagen-like proteins of Streptococcus pyogenes. The novel gene denoted sclC encodes a protein, SclC, of 302 amino acids, containing typical features found in cell wall-anchored proteins in Gram-positive bacteria. Based on similarities to the S. pyogenes collagen-like proteins the mature SclC protein can be divided into various domains: an N-terminal non-repetitive region (A), a highly repetitive collagen-like region (CL), and a C-terminal proline-rich wall-associated region (W). Using PCR, the sclC gene was detected in all studied strains of S. equi subsp. equi and S. equi subsp. zooepidemicus. Further, antibodies against recombinant SclC were detected in a collection of sera from horses with no history of strangles as well as horses previously infected with S. equi subsp. equi. Interestingly, the sera from convalescence horses were found to have significantly increased antibody titers against the SclC protein indicating that this protein is expressed during infection of S. equi subsp. equi.
Publication Date: 2004-11-27 PubMed ID: 15564026DOI: 10.1016/j.vetmic.2004.09.014Google 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.
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article discusses the identification of a new collagen-like protein, SclC, in Streptococcus equi, a bacterium causing a serious equine disease known as strangles. The findings suggest that SclC is produced during an infection and is recognised by the immune system.
Identification of SclC
The research team identified the presence of a novel collagen-like protein in Streptococcus equi, named SclC, using a technique called signal sequence phage display. This method allows the identification of genes encoding putative extracellular proteins.
- The gene identified, sclC, encodes a protein, SclC, made of 302 amino acids.
- This protein shares similarity to SclB, another collagen-like protein found in Streptococcus pyogenes.
- Analysis of this protein showed that typical features of cell wall-anchored proteins in Gram-positive bacteria are present in SclC.
Structure of SclC
The structure of the SclC protein can be divided into three main sections, akin to the collagen-like proteins found in S. pyogenes.
- The N-terminal non-repetitive region (A) which is the beginning part of the protein sequence.
- The highly repetitive collagen-like region (CL), which has a sequence that repeats over and over.
- The C-terminal proline-rich wall-associated region (W) making up the tail end of the protein sequence, which is rich in the amino acid proline and is thought to be associated with the bacterial cell wall.
Detection and Presence of SclC in Strains
The sclC gene was found in all studied strains of both S. equi subsp. equi and S. equi subsp. zooepidemicus using polymerase chain reaction (PCR).
Immune Response to SclC
The team found that antibodies against SclC were present in horses, both in those with no history of strangles and in those previously infected with S. equi subsp. equi.
- Interestingly, horses recovering from a S. equi subsp. equi infection had significantly increased levels of these antibodies.
- This observation indicates that SclC is likely expressed during S. equi subsp. equi infection and elicits a response from the host’s immune system.
Cite This Article
APA
Karlström A, Jacobsson K, Flock M, Flock JI, Guss B.
(2004).
Identification of a novel collagen-like protein, SclC, in Streptococcus equi using signal sequence phage display.
Vet Microbiol, 104(3-4), 179-188.
https://doi.org/10.1016/j.vetmic.2004.09.014 Publication
Researcher Affiliations
- Department of Microbiology, Swedish University of Agricultural Sciences, P.O. Box 7025, 750 07 Uppsala, Sweden. asa.karlstrom@mikrob.slu.se
MeSH Terms
- Amino Acid Sequence
- Animals
- Antibodies, Bacterial / blood
- Bacterial Proteins / chemistry
- Bacterial Proteins / genetics
- Bacterial Proteins / immunology
- Bacterial Proteins / isolation & purification
- Collagen / chemistry
- Electrophoresis, Polyacrylamide Gel / veterinary
- Enzyme-Linked Immunosorbent Assay / veterinary
- Horse Diseases / microbiology
- Horses
- Molecular Sequence Data
- Sequence Alignment / veterinary
- Streptococcal Infections / microbiology
- Streptococcal Infections / veterinary
- Streptococcus equi / genetics
- Streptococcus equi / immunology
- Streptococcus equi / metabolism
Citations
This article has been cited 15 times.- Dexter E, Fields PD, Ebert D. Uncovering the Genomic Basis of Infection Through Co-genomic Sequencing of Hosts and Parasites. Mol Biol Evol 2023 Jul 5;40(7).
- Lukomski S, Bachert BA, Squeglia F, Berisio R. Collagen-like proteins of pathogenic streptococci. Mol Microbiol 2017 Mar;103(6):919-930.
- Bachert BA, Choi SJ, Snyder AK, Rio RV, Durney BC, Holland LA, Amemiya K, Welkos SL, Bozue JA, Cote CK, Berisio R, Lukomski S. A Unique Set of the Burkholderia Collagen-Like Proteins Provides Insight into Pathogenesis, Genome Evolution and Niche Adaptation, and Infection Detection. PLoS One 2015;10(9):e0137578.
- Yu Z, An B, Ramshaw JA, Brodsky B. Bacterial collagen-like proteins that form triple-helical structures. J Struct Biol 2014 Jun;186(3):451-61.
- Squeglia F, Bachert B, De Simone A, Lukomski S, Berisio R. The crystal structure of the streptococcal collagen-like protein 2 globular domain from invasive M3-type group A Streptococcus shows significant similarity to immunomodulatory HIV protein gp41. J Biol Chem 2014 Feb 21;289(8):5122-33.
- Seo N, Russell BH, Rivera JJ, Liang X, Xu X, Afshar-Kharghan V, Höök M. An engineered alpha1 integrin-binding collagenous sequence. J Biol Chem 2010 Oct 1;285(40):31046-54.
- Xu C, Yu Z, Inouye M, Brodsky B, Mirochnitchenko O. Expanding the family of collagen proteins: recombinant bacterial collagens of varying composition form triple-helices of similar stability. Biomacromolecules 2010 Feb 8;11(2):348-56.
- Guss B, Flock M, Frykberg L, Waller AS, Robinson C, Smith KC, Flock JI. Getting to grips with strangles: an effective multi-component recombinant vaccine for the protection of horses from Streptococcus equi infection. PLoS Pathog 2009 Sep;5(9):e1000584.
- Yoshizumi A, Yu Z, Silva T, Thiagarajan G, Ramshaw JA, Inouye M, Brodsky B. Self-association of streptococcus pyogenes collagen-like constructs into higher order structures. Protein Sci 2009 Jun;18(6):1241-51.
- Caswell CC, Barczyk M, Keene DR, Lukomska E, Gullberg DE, Lukomski S. Identification of the first prokaryotic collagen sequence motif that mediates binding to human collagen receptors, integrins alpha2beta1 and alpha11beta1. J Biol Chem 2008 Dec 26;283(52):36168-75.
- Hamilton A, Robinson C, Sutcliffe IC, Slater J, Maskell DJ, Davis-Poynter N, Smith K, Waller A, Harrington DJ. Mutation of the maturase lipoprotein attenuates the virulence of Streptococcus equi to a greater extent than does loss of general lipoprotein lipidation. Infect Immun 2006 Dec;74(12):6907-19.
- Mullen LM, Nair SP, Ward JM, Rycroft AN, Henderson B. Phage display in the study of infectious diseases. Trends Microbiol 2006 Mar;14(3):141-7.
- Kelly C, Bugg M, Robinson C, Mitchell Z, Davis-Poynter N, Newton JR, Jolley KA, Maiden MC, Waller AS. Sequence variation of the SeM gene of Streptococcus equi allows discrimination of the source of strangles outbreaks. J Clin Microbiol 2006 Feb;44(2):480-6.
- Lannergård J, Flock M, Johansson S, Flock JI, Guss B. Studies of fibronectin-binding proteins of Streptococcus equi. Infect Immun 2005 Nov;73(11):7243-51.
- Huessy B, Bumann D, Ebert D. Ectopical expression of bacterial collagen-like protein supports its role as adhesin in host-parasite coevolution. R Soc Open Sci 2024 Apr;11(4):231441.
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