Occurrence of the M Substance of Type 28 Group A in Streptococci of Lancefield Groups B, G and G

Maxted, W. R.

doi:10.1099/00221287-3-1-1

Cited by 38 publications

(21 citation statements)

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“…Our results also show that RD2-like regions are present in multiple Lancefield group C and group G strains, additional evidence for horizontal dissemination of RD2 in natural populations of streptococci. Of note, the detection of an RD2-like element in group B [16], C and G streptococci (this work) is consistent with early reports of the production of the R28 antigen in these organisms [5,36]. …”

Section: Discussionsupporting

confidence: 90%

Lateral gene transfer of streptococcal ICE element RD2 (region of difference 2) encoding secreted proteins

et al. 2011

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BackgroundThe genome of serotype M28 group A Streptococcus (GAS) strain MGAS6180 contains a novel genetic element named Region of Difference 2 (RD2) that encodes seven putative secreted extracellular proteins. RD2 is present in all serotype M28 strains and strains of several other GAS serotypes associated with female urogenital infections. We show here that the GAS RD2 element is present in strain MGAS6180 both as an integrative chromosomal form and a circular extrachromosomal element. RD2-like regions were identified in publicly available genome sequences of strains representing three of the five major group B streptococcal serotypes causing human disease. Ten RD2-encoded proteins have significant similarity to proteins involved in conjugative transfer of Streptococcus thermophilus integrative chromosomal elements (ICEs).ResultsWe transferred RD2 from GAS strain MGAS6180 (serotype M28) to serotype M1 and M4 GAS strains by filter mating. The copy number of the RD2 element was rapidly and significantly increased following treatment of strain MGAS6180 with mitomycin C, a DNA damaging agent. Using a PCR-based method, we also identified RD2-like regions in multiple group C and G strains of Streptococcus dysgalactiae subsp.equisimilis cultured from invasive human infections.ConclusionsTaken together, the data indicate that the RD2 element has disseminated by lateral gene transfer to genetically diverse strains of human-pathogenic streptococci.

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Section: Discussionsupporting

confidence: 90%

Lateral gene transfer of streptococcal ICE element RD2 (region of difference 2) encoding secreted proteins

et al. 2011

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“…Rarely, a T antigen occurring in a Group A type has also been found in a type within another streptococcal group, for example, as noted by Grifl~th, Group A, Type 2 and Group C, Type 21 (9). R antigen, however, which was first found in Group A Type 28 strains, occurs in some members of three types of Group A streptococci, as well as in certain strains of Groups B, C, and G (13). Originally this antigen, on the basis of precipitin reactions which seemed to indicate that it was an M antigen, was considered to be the type-specific antigen of Type 28.…”

Section: Discussionmentioning

confidence: 99%

Occurrence of R Antigen Specific for Group a Type 3 Streptococci

Lancefield

1958

The Journal of Experimental Medicine

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Three different protein antigens, designated by the letters M, T, and R, have been shown to be present on the surface of Group A streptococci (1). With respect to streptococcal infections the M antigens are the most important, since they are essential to the virulence of the microorganisms and stimulate the production of protective antibodies in the infected or immunized animal. Accordingly, the M antigens were selected as the basis for classification of Group A streptococci into serological types.The serological type of a given Group A streptococcus is usually determined by specific precipitin tests for M antigen. Other immunological reactions dependent upon this antigen-antibody system can also be used for identification of either M antigen or its antibody. Thus, under appropriate conditions the following procedures have been used to obtain information about the type-specific reactions of M antigens and their antibodies: agglutination reactions, active and passive protection tests, anaphylaxis experiments, bactericidal tests dependent upon phagocytosis of sensitized streptococci, and occasionally complement fixation tests (2).In those cases in which precipitin or agglutination tests give equivocal results in attempted identification of the M antigen, definitive information can be derived from the more biological mouse protection and bactericidal tests. Thus, T antigens, which cause confusion in agglutination tests for type specificity, can be clearly differentiated from M antigens by protection or bactericidal tests. Similarly, these procedures serve to establish the fact that 28 R antigen is not one of the M proteins.The present report concerns a newly identified antigen found in certain Type 3 strains. The experiments reported in this paper show that it is not an M antigen. So far it has not been found in any other type or group of streptococci, but only in Group A streptococci, Type 3. Since this antigen, like the 28 R antigen, appears to represent another protein antigen which can interfere

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“…Group G organisms are found as part of the normal flora of the skin, upper respiratory tract, and female genital tract. However, these organisms are responsible for an increasing number of human diseases (4,6,142).…”

Section: Homology Of M Protein With Other Molecules Of Gram-positive mentioning

confidence: 99%

Streptococcal M protein: molecular design and biological behavior

1989

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M protein is a major virulence determinant for the group A streptococcus by virtue of its ability to allow the organism to resist phagocytosis. Common in eucaryotes, the fibrillar coiled-coil design for the M molecule may prove to be a common motif for surface proteins in gram-positive organisms. This type of structure offers the organism several distinct advantages, ranging from antigenic variation to multiple functional domains. The close resemblance of this molecular design to that of certain mammalian proteins could help explain on a molecular level the formation of epitopes responsible for serological cross-reactions between microbial and mammalian proteins. Many of the approaches described in the elucidation of the M-protein structure may be applied for characterizing similar molecules in other microbial systems.

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Occurrence of the M Substance of Type 28 Group A in Streptococci of Lancefield Groups B, G and G

Cited by 38 publications

References 1 publication

Lateral gene transfer of streptococcal ICE element RD2 (region of difference 2) encoding secreted proteins

Lateral gene transfer of streptococcal ICE element RD2 (region of difference 2) encoding secreted proteins

Occurrence of R Antigen Specific for Group a Type 3 Streptococci

Streptococcal M protein: molecular design and biological behavior

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