THE Ibc PROTEIN FRACTION OF GROUP B STREPTOCOCCI: CHARACTERIZATION OF PROTEIN ANTIGENS EXTRACTED BY HC1

Author(s):  
LARS BEVANGER ◽  
OLE-JAN IVERSEN
1988 ◽  
Vol 10 (Supplement 2) ◽  
pp. S367-S371 ◽  
Author(s):  
D. G. Pritchard ◽  
M. L. Egan ◽  
B. M. Gray ◽  
H. C. Dillon

1991 ◽  
Vol 59 (6) ◽  
pp. 2023-2028 ◽  
Author(s):  
J L Michel ◽  
L C Madoff ◽  
D E Kling ◽  
D L Kasper ◽  
F M Ausubel

1990 ◽  
Vol 20 (10) ◽  
pp. 2241-2247 ◽  
Author(s):  
Gunnar Lindahl ◽  
Bo Åkerström ◽  
Jean-Pierre Vaerman ◽  
Lars Stenberg

2009 ◽  
Vol 16 (9) ◽  
pp. 1302-1308 ◽  
Author(s):  
Rooyen T. Mavenyengwa ◽  
Johan A. Maeland ◽  
Sylvester R. Moyo

ABSTRACTGroup B streptococci (GBS) express a variety of surface-exposed and strain-variable proteins which function as phenotypic markers and as antigens which are able to induce protective immunity in experimental settings. Among these proteins, the chimeric and immunologically cross-reacting alpha-like proteins are particularly important. Another protein, R3, which has been less well studied, occurred at a frequency of 21.5% in GBS from Zimbabwe and, notably, occurred in serotype V strains at a frequency of 75.9%. Working with rabbit antiserum raised against the R3 reference strain ATCC 49447 (strain 10/84; serotype V/R3) to detect the expression of the R3 protein, we recorded findings which suggested that strain 10/84 expressed a strain-variable protein antigen, in addition to R3. The antigen was detected by various enzyme-linked immunosorbent assay-based tests by using acid extract antigens or GBS whole-cell coats and by whole-cell-based Western blotting. We named the putative novel antigen the Z antigen. The Z antigen was a high-molecular-mass antigen that was susceptible to degradation by pepsin and trypsin but that was resistant tom-periodate oxidation and failed to show immunological cross-reactivity with any of a variety of other GBS protein antigens. The Z antigen was expressed by 33/121 (27.2%) of strains of a Zimbabwean GBS strain collection and by 64.2% and 72.4% of the type Ib and type V strains, respectively, and was occasionally expressed by GBS of other capsular serotypes. Thus, the putative novel GBS protein named Z showed distinct capsular antigen associations and presented as an important phenotypic marker in GBS from Zimbabwe. It may be an important antigen in GBS from larger areas of southern Africa. Its prevalence in GBS from Western countries is not known.


2003 ◽  
Vol 49 (5) ◽  
pp. 350-356 ◽  
Author(s):  
Kyle N Seifert ◽  
William P McArthur ◽  
Arnold S Bleiweis ◽  
L Jeannine Brady

During characterization of the surface antigens of serotype III group B streptococci (GBS), a protein with an apparent Mr~ 173 500 migrating on a SDS – polyacrylamide gel was found to have an N-terminal amino acid sequence identical to that of the plasmin receptor (Plr) of group A streptococci, a surface-localized glyceraldehyde-3-phosphate dehydrogenase (GAPDH). This work begins to characterize GBS GAPDH and to assess its functional activity on the cell surface. The 1.0-kb gapC gene of GBS was amplified by PCR. plr and gapC demonstrated 87% homology. An anti-Plr monoclonal antibody reacted with GBS whole cells, suggesting GBS GAPDH is surface localized. Multiple serotypes of GBS demonstrated functional GAPDH on their surfaces. The anti-Plr monoclonal antibody recognized GBS protein bands of approximately 41 and 173.5 kDa, by Western blot. Presumably, these represent monomeric and tetrameric forms of the GAPDH molecule. GBS GAPDH was demonstrated by Western blot analysis to interact with lys- and glu-plasminogens. Fluid-phase GBS GAPDH interacted, by means of ELISA, with immobilized lys-plasminogen, glu-plasminogen, actin, and fibrinogen. Enzymatically active GAPDH, capable of binding cytoskeletal and extracellular matrix proteins, is expressed on the surface of GBS.Key words: group B streptococci, glyceraldehyde-3-phosphate dehydrogenase.


2016 ◽  
Vol 54 (7) ◽  
pp. 1932-1932
Author(s):  
Anne Six ◽  
Arnaud Firon ◽  
Céline Plainvert ◽  
Camille Caplain ◽  
Abdelouhab Bouaboud ◽  
...  

2016 ◽  
Vol 99 ◽  
pp. 119-122 ◽  
Author(s):  
Mohammad Emaneini ◽  
Fereshteh Jabalameli ◽  
Akbar Mirsalehian ◽  
Amir Ghasemi ◽  
Reza Beigverdi

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