A unique serine-rich repeat protein (Srr-2) and novel surface antigen (epsilon) associated with a virulent lineage of serotype III Streptococcus agalactiae

Microbiology (Reading). 2006 Apr;152(Pt 4):1029-1040. doi: 10.1099/mic.0.28516-0.

Abstract

Group B streptococci (GBS) are pathogens of both neonates and adults, with serotype III strains in particular being associated with invasive disease and meningitis. In this study, a novel GBS surface antigen, epsilon, was found to be co-expressed with the previously reported delta antigen on an identical subset of serotype III GBS. Expression of delta/epsilon on the surface of serotype III GBS was shown to distinguish the restriction digest pattern (RDP) III-3 and multilocus sequence typing (ST)-17 lineage. epsilon-Specific antibodies were reactive with a unique, high-molecular-mass, serine-rich repeat protein (Srr-2) found exclusively in RDP III-3 strains. The gene encoding Srr-2 was located within a putative accessory secretory locus that included secY2 and secA2 homologues and had a genetic organization similar to that of the secY2/A2 locus of staphylococci. In contrast, serotype III delta/epsilon-negative strains and strains representative of serotypes Ia, Ib, Ic and II shared a common Srr-encoding gene, srr-1, and an organization of the secY2/A2 locus similar to that of previously reported serotype Ic, delta/epsilon-negative serotype III and serotype V GBS strains. Representative serotype III delta/epsilon-positive strains had LD(90) values 3-4 logs less than those of serotype III delta/epsilon-negative strains in a neonatal mouse model of infection. These results indicate that the RDP III-3/ST-17 lineage expresses Srr-2 and is highly virulent in an in vivo model of neonatal sepsis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Animals
  • Antigens, Bacterial / analysis*
  • Antigens, Bacterial / genetics
  • Bacterial Proteins / analysis*
  • Bacterial Proteins / genetics
  • DNA Fingerprinting
  • DNA, Bacterial / genetics
  • Disease Models, Animal
  • Humans
  • Membrane Proteins / analysis*
  • Membrane Proteins / genetics
  • Membrane Transport Proteins / genetics
  • Mice
  • Molecular Sequence Data
  • Polymorphism, Restriction Fragment Length
  • SEC Translocation Channels
  • SecA Proteins
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Staphylococcus / genetics
  • Streptococcal Infections / microbiology
  • Streptococcus agalactiae / chemistry*
  • Streptococcus agalactiae / classification
  • Streptococcus agalactiae / genetics
  • Streptococcus agalactiae / pathogenicity*
  • Survival Analysis
  • Virulence Factors / analysis
  • Virulence Factors / genetics*

Substances

  • Antigens, Bacterial
  • Bacterial Proteins
  • DNA, Bacterial
  • Membrane Proteins
  • Membrane Transport Proteins
  • SEC Translocation Channels
  • Virulence Factors
  • Adenosine Triphosphatases
  • SecA Proteins

Associated data

  • GENBANK/AY669067
  • GENBANK/DQ174691