Two major classes in the M protein family in group A streptococci

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TY  - JOUR
  - O'Toole, P. W. and O'Toole, P. and Stenberg, L. and Rissler, M. and Lindahl, G.
  - 1992
  - January
  - Proc Natl Acad Sci U S A
  - Two major classes in the M protein family in group A streptococci
  - Validated
  - 89
  - 18
  - 8661
  - 5
  - The M protein family of molecules in the group A streptococcus comprises a number of cell surface proteins that interact with the immune system of the host. One of the proteins in this family is the IgA receptor Arp4, which has C repeats similar to those that characterize the known M proteins. The streptococcal strain expressing Arp4 also expresses a second immunoglobulin-binding protein, Mrp4, which is shown here to be encoded by a gene located immediately upstream of the gene for Arp4. In addition to binding IgG, Mrp4 also binds fibrinogen, a property ascribed to M proteins. DNA sequence analysis demonstrated that the Mrp4 protein indeed is a member of the M protein family, but it was unexpectedly found to have a type of repeat that is identical to the A repeat described for FcRA76, a partially sequenced streptococcal Fc receptor. Purified FcRA76 was shown to bind fibrinogen and IgG, like Mrp4. These data show that the known molecules in the M protein family can be divided into two classes, A and C, according to the type of repeat region found. Hybridization studies with a panel of clinical isolates indicate that many streptococcal strains express class A and class C proteins, whereas some strains express only class C proteins. Class A molecules show amino-terminal sequence variation, like class C molecules, which suggests that proteins of both classes are targets for the immune response.
  - http://www.ncbi.nlm.nih.gov/pubmed/1528877
  - 10.1073/pnas.89.18.8661
DA  - 1992/01
ER  - 
@article{V277480629,
   = {O'Toole, P. W. and O'Toole, P. and Stenberg, L. and Rissler, M. and Lindahl, G.},
   = {1992},
   = {January},
   = {Proc Natl Acad Sci U S A},
   = {Two major classes in the M protein family in group A streptococci},
   = {Validated},
   = {89},
   = {18},
  pages = {8661--5},
   = {{The M protein family of molecules in the group A streptococcus comprises a number of cell surface proteins that interact with the immune system of the host. One of the proteins in this family is the IgA receptor Arp4, which has C repeats similar to those that characterize the known M proteins. The streptococcal strain expressing Arp4 also expresses a second immunoglobulin-binding protein, Mrp4, which is shown here to be encoded by a gene located immediately upstream of the gene for Arp4. In addition to binding IgG, Mrp4 also binds fibrinogen, a property ascribed to M proteins. DNA sequence analysis demonstrated that the Mrp4 protein indeed is a member of the M protein family, but it was unexpectedly found to have a type of repeat that is identical to the A repeat described for FcRA76, a partially sequenced streptococcal Fc receptor. Purified FcRA76 was shown to bind fibrinogen and IgG, like Mrp4. These data show that the known molecules in the M protein family can be divided into two classes, A and C, according to the type of repeat region found. Hybridization studies with a panel of clinical isolates indicate that many streptococcal strains express class A and class C proteins, whereas some strains express only class C proteins. Class A molecules show amino-terminal sequence variation, like class C molecules, which suggests that proteins of both classes are targets for the immune response.}},
   = {http://www.ncbi.nlm.nih.gov/pubmed/1528877},
   = {10.1073/pnas.89.18.8661},
  source = {IRIS}
}
AUTHORSO'Toole, P. W. and O'Toole, P. and Stenberg, L. and Rissler, M. and Lindahl, G.
YEAR1992
MONTHJanuary
JOURNALProc Natl Acad Sci U S A
TITLETwo major classes in the M protein family in group A streptococci
STATUSValidated
PEER_REVIEW
SEARCH_KEYWORD
VOLUME89
ISSUE18
START_PAGE8661
END_PAGE5
ABSTRACTThe M protein family of molecules in the group A streptococcus comprises a number of cell surface proteins that interact with the immune system of the host. One of the proteins in this family is the IgA receptor Arp4, which has C repeats similar to those that characterize the known M proteins. The streptococcal strain expressing Arp4 also expresses a second immunoglobulin-binding protein, Mrp4, which is shown here to be encoded by a gene located immediately upstream of the gene for Arp4. In addition to binding IgG, Mrp4 also binds fibrinogen, a property ascribed to M proteins. DNA sequence analysis demonstrated that the Mrp4 protein indeed is a member of the M protein family, but it was unexpectedly found to have a type of repeat that is identical to the A repeat described for FcRA76, a partially sequenced streptococcal Fc receptor. Purified FcRA76 was shown to bind fibrinogen and IgG, like Mrp4. These data show that the known molecules in the M protein family can be divided into two classes, A and C, according to the type of repeat region found. Hybridization studies with a panel of clinical isolates indicate that many streptococcal strains express class A and class C proteins, whereas some strains express only class C proteins. Class A molecules show amino-terminal sequence variation, like class C molecules, which suggests that proteins of both classes are targets for the immune response.
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URLhttp://www.ncbi.nlm.nih.gov/pubmed/1528877
DOI_LINK10.1073/pnas.89.18.8661
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