| Literature DB >> 29106586 |
Shun-Mei Lin1,2, A-Yeung Jang1,3, Yong Zhi1,4, Shuang Gao1,2, Sangyong Lim1,4, Jae Hyang Lim4, Joon Young Song5, Paul M Sullam6,7,8,9, Joon Haeng Rhee2,10,11, Ho Seong Seo1,4.
Abstract
Streptococcus agalactiae (group B streptococcus [GBS]) is a leading cause of invasive diseases in neonates and severe infections in elderly individuals. GBS serine-rich repeat glycoprotein 1 (Srr1) acts as a critical virulence factor by facilitating GBS invasion into the central nervous system through interaction with the fibrinogen Aα chain. This study revealed that srr1 is highly conserved, with 86.7% of GBS clinical isolates expressing the protein. Vaccination of mice with different Srr1 truncated peptides revealed that only Srr1 truncates containing the latch domain protected against GBS meningitis. Furthermore, the latch peptide alone was immunogenic and elicited protective antibodies, which efficiently enhanced antibody-mediated opsonophagocytic killing of GBS by HL60 cells and provided heterogeneous protection against 4 different GBS serogroups. Taken together, these findings indicated that the latch domain of Srr1 may constitute an effective peptide vaccine candidate for GBS.Entities:
Keywords: Streptococcus agalactiae; latch; serine-rich repeat; vaccine
Mesh:
Substances:
Year: 2017 PMID: 29106586 PMCID: PMC5854025 DOI: 10.1093/infdis/jix565
Source DB: PubMed Journal: J Infect Dis ISSN: 0022-1899 Impact factor: 5.226