Immunologically reactive proteins of Streptococcus equi.
Abstract: Immunologically reactive proteins in acid extracts and culture supernatants of Streptococcus equi were recognized through a combination of chromatographic and immunologic procedures. Both high- and low-molecular-weight components of each of these protein preparations were protective for mice and were, therefore, presumed to contain a variety of hydrolytic products or fragments of the M protein of S. equi. Convalescent horse sera that exhibited strong bactericidal activity for S. equi always reacted with polypeptides in the molecular weight range of 24,000 to 29,000, whereas preinfection sera did not. Rabbit antisera to affinity-purified S. equi protein also reacted with these polypeptides, as well as with a polypeptide of about 36,000 to 37,000 molecular weight. M protein in acid extract and culture supernatant did not cross-react in immunodiffusion, but rabbit antiserum to affinity-purified M protein from an acid extract of S. equi reacted strongly with culture supernatant proteins of approximate molecular weights of 67,000, 58,000, and 43,000. We suggest, therefore, that the M protein in culture supernatant is masked by other sequences that are removed by hot acid during preparation of acid extracts. Polypeptides common to acid extracts of S. equi and Streptococcus zooepidemicus were also identified. These polypeptides had molecular weights of about 55,000 and 31,000.
Publication Date: 1985-04-01 PubMed ID: 3980091PubMed Central: PMC261909DOI: 10.1128/iai.48.1.29-34.1985Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- Non-P.H.S.
Summary
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This research work explores proteins found in Streptococcus equi, a type of bacteria, and their role in immune response. The study finds various proteins that foster protection in mice against the bacteria and suggests that M protein, a key molecule, may be concealed by other sequences in the bacterial culture.
Research Methods and Findings
The study looked at immunologically reactive proteins. The techniques used were chromatographic and immunologic procedures, which enabled the detection of proteins in acid extracts and culture supernatants of Streptococcus equi. Specific findings included:
- Both high and low molecular weight components of the protein preparations were found to be protective in mice. This suggests that they may contain a variety of hydrolytic products or fragments of the M protein of S. equi.
- Convalescent horse sera – the blood serum from horses recovering from an infection – that displayed strong bactericidal activity for S. equi reacted with polypeptides in the molecular weight range of 24,000 to 29,000.
- In contrast, preinfection sera did not react with these polypeptides.
- Rabbit antisera to affinity-purified S. equi protein also reacted with these polypeptides, as well as with a polypeptide of about 36,000 to 37,000 molecular weight.
M protein Interaction
The researchers observed the M protein in two forms:
- In acid extract and culture supernatant, the M protein did not cross-react in immunodiffusion.
- Rabbit antiserum to affinity-purified M protein from an acid extract of S. equi reacted strongly with culture supernatant proteins of approximate molecular weights of 67,000, 58,000, and 43,000.
This led the researchers to propose that the M protein in culture supernatant could be hidden by other protein sequences, which are removed by hot acid during the preparation of acid extracts.
Identification of Common Polypeptides
Another significant finding was the identification of common polypeptides in the acid extracts of both S. equi and Streptococcus zooepidemicus. These polypeptides had molecular weights of about 55,000 and 31,000. This suggests that there might be similar immune responses prompted by these bacteria and potentially similar methods for strategic targeting for therapy or prevention.
Cite This Article
APA
Timoney JF, Trachman J.
(1985).
Immunologically reactive proteins of Streptococcus equi.
Infect Immun, 48(1), 29-34.
https://doi.org/10.1128/iai.48.1.29-34.1985 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Antigens, Bacterial / analysis
- Bacterial Outer Membrane Proteins
- Bacterial Proteins / analysis
- Carrier Proteins
- Chromatography, Gel
- Horses / microbiology
- Mice
- Mice, Inbred ICR
- Molecular Weight
- Streptococcus / immunology
References
This article includes 15 references
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Citations
This article has been cited 7 times.- Timoney JF, Suther P, Velineni S, Artiushin SC. The Antiphagocytic Activity of SeM of Streptococcus equi Requires Capsule.. J Equine Sci 2014;25(2):53-6.
- Lewis MJ, Meehan M, Owen P, Woof JM. A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system.. J Biol Chem 2008 Jun 20;283(25):17615-23.
- Harrington DJ, Greated JS, Chanter N, Sutcliffe IC. Identification of lipoprotein homologues of pneumococcal PsaA in the equine pathogens Streptococcus equi and Streptococcus zooepidemicus.. Infect Immun 2000 Oct;68(10):6048-51.
- Boschwitz JS, Timoney JF. Inhibition of C3 deposition on Streptococcus equi subsp. equi by M protein: a mechanism for survival in equine blood.. Infect Immun 1994 Aug;62(8):3515-20.
- Timoney JF, Walker J, Zhou M, Ding J. Cloning and sequence analysis of a protective M-like protein gene from Streptococcus equi subsp. zooepidemicus.. Infect Immun 1995 Apr;63(4):1440-5.
- Galán JE, Timoney JF. Immunologic and genetic comparison of Streptococcus equi isolates from the United States and Europe.. J Clin Microbiol 1988 Jun;26(6):1142-6.
- Galán JE, Timoney JF. Molecular analysis of the M protein of Streptococcus equi and cloning and expression of the M protein gene in Escherichia coli.. Infect Immun 1987 Dec;55(12):3181-7.
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