Immunochemical Characterization of the Polysaccharide Antigens of Group B Streptococci

1988 ◽  
Vol 10 (Supplement 2) ◽  
pp. S367-S371 ◽  
Author(s):  
D. G. Pritchard ◽  
M. L. Egan ◽  
B. M. Gray ◽  
H. C. Dillon
1990 ◽  
Vol 20 (10) ◽  
pp. 2241-2247 ◽  
Author(s):  
Gunnar Lindahl ◽  
Bo Åkerström ◽  
Jean-Pierre Vaerman ◽  
Lars Stenberg

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

Author(s):  
Rajwent Singh ◽  
A.K. Arora ◽  
T.S. Rai ◽  
Mudit Chandra

Background: Group B streptococcus (GBS) or Streptococcus agalactiae is an important pathogen associated with bovine mastitis. The organism is also of public health consequences and may cause variety of infections ranging from neonatal sepsis, pneumonia and meningitis to localized infections and urinary tract infection or arthritisin adult humans. Widespread use of antibiotics in veterinary medicine has led to development of resistance among the pathogens. So there is need for surveillance of antimicrobial resistance to ensure effective treatment. Methods: Milk samples collected from mastitis affected animals were processed for isolation of Streptococcus agalactiae. The isolates were tested for antimicrobial susceptibility. Molecular characterisation was carried out by PCR to study the occurrence of resistance marker genes and virulence marker genes. RAPD was carried out to study genetic diversity among the isolates. Result: Six isolates of S. agalactiae were obtained from 182 milk samples. Highest resistance was observed against co-trimoxazole and tetracycline followed by ampicillin. tetM gene and tetO genes could be amplified in four and three isolates, respectively. None of the isolates showed amplification for ermA, ermB, mefA and mefE genes. Three isolates were positive for the five virulence genes tested (glnA, cfb, hylB, scaA and cyl). RAPD analysis demonstrated great intraspecific genetic diversity among the streptococcal isolates.


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