Human pathogenic streptococcal proteomics and vaccine development

Abstract

Gram-positive streptococci are non-motile, chain-forming bacteria commonly found in the normal oral and bowel flora of warm-blooded animals. Over the past decade, a proteomic approach combining 2-DE and MS has been used to systematically map the cellular, surface-associated and secreted proteins of human pathogenic streptococcal species. The public availability of complete streptococcal genomic sequences and the amalgamation of proteomic, genomic and bioinformatic technologies have recently facilitated the identification of novel streptococcal vaccine candidate antigens and therapeutic agents. The objective of this review is to examine the constituents of the streptococcal cell wall and secreted proteome, the mechanisms of transport of surface and secreted proteins, and describe the current methodologies employed for the identification of novel surface-displayed proteins and potential vaccine antigens.

Conserved anchorless surface proteins as group A streptococcal vaccine candidates

“…Although several surface proteins and virulence factors have been previously assessed as vaccine candidates [34], there is no commercial vaccine available to prevent GAS infection. Following a proteomic analysis of an M1T1 cell wall extract, we selected three anchorless proteins; ADI, FBA and TF; for further characterization as putative GAS vaccine candidates.…”

“…Several previously characterized GAS vaccine candidates; M protein, SfbI, SOF and FbaA [34] are not conserved between GAS serotypes nor expressed by all serotypes of GAS. The genes encoding each of the anchorless vaccine antigens of this study were ubiquitous amongst sequenced GAS genomes with  99% conservation amongst serotypes ( Table 2).…”

Comparative Proteomic Analysis of Extracellular Proteins of Clostridium perfringens Type A and Type C Strains

“…For MALDI-TOF mass spectrometry, 1 l of the digest was mixed with 2 l of the matrix solution (5 mg ␣-cyano-4-hydroxycinnamic acid in 80% [vol/vol] acetonitrile and 0.1% [wt/vol] trifluoroacetic acid [TFA]), and 1 l of this mixture was deposited onto the MALDI target. The spectrum was obtained in the mass range of 500 to 4,000 Da and was calibrated using a calibration mixture containing angiotensin I, Substance P, adrenocorticotropin (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17) [ACTH(1-17)], ACTH , and somatostatin (28).…”

Group A Streptococcal Cysteine Protease Cleaves Epithelial Junctions and Contributes to Bacterial Translocation

“…Despite the availability of sequence information for several GAS genomes and detailed characterization of their virulence factors, a safe and effective commercial GAS vaccine has yet to be developed (3).…”