Molecular Diversity Among the Trypsin Resistant Surface Proteins of Group B Streptococc

Flores, Aurea E.; Ferrieri, Patricia

doi:10.1016/s0934-8840(96)80021-1

Cited by 25 publications

(28 citation statements)

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“…GBS isolates were subcultured onto 5% sheep blood agar plates (BAPs) and grown at 37°C overnight in Todd-Hewitt broth (BD, Sparks, MD) for serotyping or for 48 h on BAPs for PFGE analysis (5). The isolates were stored at Ϫ30°C in Todd-Hewitt broth with 2% defibrinated sheep blood (14,17,40).…”

Section: Methodsmentioning

confidence: 99%

“…The capsular polysaccharide type and protein profile were determined for each isolate by using HCl extraction and Ouchterlony double immunodiffusion with rabbit antisera monospecific for CPS type or surface protein as we have previously described (14,17,24,40). Proteins under study in our laboratory included c(␣), c(␤), R1, R4(Rib), R1,R4 (known as Alp3), and BPS (47).…”

Section: Methodsmentioning

confidence: 99%

“…HCl extracts were concentrated 3-fold and retested when a reaction was weak or inconclusive. Prototype strains for the surface proteins were the ones used in our previous studies; strain 3139 (S. Bergner-Rabinowitz, Israel), which did not express any of these proteins, was the CPS type IV prototype (14,17,24).…”

Section: Methodsmentioning

confidence: 99%

“…Isolates that do not express any of the known CPS types are designated nontypeable (NT) (2,6,21,40). In addition to CPS, GBS may express one or more surface-localized proteins, including the ␣ and ␤ components of the c protein (24); the alpha-like R proteins, specifically R1, R4(Rib), and R1,R4 (also known as Alp3) (14,17,19,30,40); and the group B protective surface (BPS) protein (12). Certain protein profiles are associated with each capsular polysaccharide CPS type (2), for example, the c(␣ only) protein with types Ia and II, c(␣ ϩ ␤) with type Ib, and R4(Rib) with type III (2,14).…”

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confidence: 99%

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Clonal Analysis of Colonizing Group B Streptococcus , Serotype IV, an Emerging Pathogen in the United States

et al. 2010

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Colonizing group B Streptococcus (GBS) capsular polysaccharide (CPS) type IV isolates were recovered from vaginal and rectal samples obtained from 97 (8.4%) nonpregnant women of 1,160 women enrolled in a U.S. multicenter GBS vaccine study from 2004 to 2008. Since this rate was much higher than the rate of prevalence of 0.4 to 0.6% that we found in previous studies, the isolates were analyzed by using surface protein profile identification, pulsed-field gel electrophoresis (PFGE), and multilocus sequence typing (MLST) to characterize them and identify trends in DNA clonality and divergence. Of the 101 type IV isolates studied, 53 expressed ␣ and group B protective surface (BPS) proteins, 27 expressed BPS only, 20 expressed ␣ only, and 1 had no detectable surface proteins. The isolates spanned three PFGE macrorestriction profile groups, groups 37, 38, and 39, of which group 37 was predominant. The isolates in group 37 expressed the ␣ and BPS proteins, while those in groups 38 and 39 expressed the ␣ protein only, with two exceptions. MLST studies of selective isolates from the four protein profile groups showed that isolates expressing ␣,BPS or BPS only were of a new sequence type, sequence type 452, while those expressing ␣ only or no proteins were mainly of a new sequence type, sequence type 459. Overall, our study revealed a limited diversity in surface proteins, MLST types, and DNA macrorestriction profiles for type IV GBS. There appeared to be an association between the MLST types and protein expression profiles. The increased prevalence of type IV GBS colonization suggested the possibility that this serotype may emerge as a GBS pathogen.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Clonal Analysis of Colonizing Group B Streptococcus , Serotype IV, an Emerging Pathogen in the United States

et al. 2010

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“…R proteins from GBS strains were detected in agarose slides by Ouchterlony double-diffusion (DD) immunoprecipitation using Lancefield hot HCl or 0.1% trypsin cell extracts (11). To examine the susceptibilities of the various R proteins to trypsin or pepsin digestion, HCl or 0.1% trypsin cell extracts were treated (1 h at 37°C; pH 8.2) either with 5 or 0.2% trypsin or with 0.5 or 0.2% pepsin (pH 2.0 and 4.0, respectively) (11,38,44,45). Enzyme-treated or control (buffer only) samples were then tested to determine the effects of such treatments on the immunoprecipitation reactions.…”

Section: Methodsmentioning

confidence: 99%

Molecular Analysis of Group B Protective Surface Protein, a New Cell Surface Protective Antigen of Group B Streptococci

et al. 2002

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Group B streptococci (GBS) express various surface antigens designated c, R, and X antigens. A new R-like surface protein from Streptococcus agalactiae strain Compton R has been identified by using a polyclonal antiserum raised against the R protein fraction of this strain to screen a lambda Zap library. DNA sequence analysis of positive clones allowed the prediction of the primary structure of a 105-kDa protein designated BPS protein (group B protective surface protein) that exhibited typical features of streptococcal surface proteins such as a signal sequence and a membrane anchor region but did not show significant similarity with other known sequences. Immunogold electron microscopy using a BPS-specific antiserum confirmed the surface location of BPS protein on S. agalactiae strain Compton R. Anti-BPS antibodies did not cross-react with R1 and R4 proteins expressed by two variant type III GBS strains but reacted with the parental streptococcal strain in Western blot and immunoprecipitation analyses. Separate R3 and BPS immunoprecipitation bands were observed when a cell extract of strain Compton R was tested with an antiserum against Compton R previously cross-absorbed to remove R4 antibodies. Immunization of mice with recombinant BPS protein by the subcutaneous route produced an efficient antigen-specific response, and immunized animals survived challenge with a lethal dose of a virulent strain. Therefore, BPS protein represents a new R-like protective antigen of GBS.

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Medically Important Beta-Hemolytic Streptococci

Cleary¹,

Cheng²

2006

The Prokaryotes

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Molecular Diversity Among the Trypsin Resistant Surface Proteins of Group B Streptococc

Cited by 25 publications

References 15 publications

Clonal Analysis of Colonizing Group B Streptococcus , Serotype IV, an Emerging Pathogen in the United States

Clonal Analysis of Colonizing Group B Streptococcus , Serotype IV, an Emerging Pathogen in the United States

Molecular Analysis of Group B Protective Surface Protein, a New Cell Surface Protective Antigen of Group B Streptococci

Medically Important Beta-Hemolytic Streptococci

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