Secreted surface-localized effector (SslE) (SslE)

Secreted surface-localized effector (SslE), also known as YghJ, is a large lipoprotein and M60-like metalloprotease secreted by the Type II secretion system (T2SS) in various pathogenic Escherichia coli strains, including Enterotoxigenic E. coli (ETEC) and Extraintestinal pathogenic E. coli (ExPEC) (UniProt P0ADK8). Its primary biological function involves the degradation of host mucins, such as MUC2, MUC3, and MUC5AC, which facilitates bacterial penetration of the protective mucus layer and subsequent colonization of the host epithelium (Luo et al., 2014). SslE is highly conserved across diverse E. coli pathotypes and plays a critical role in biofilm maturation, making it a significant virulence factor (Nesta et al., 2014). Due to its surface accessibility and conservation, SslE is a leading candidate for the development of broadly protective vaccines against E. coli-associated diseases like diarrhea, urinary tract infections, and neonatal meningitis (Moriel et al., 2010). While no small-molecule inhibitors are currently in clinical use, experimental studies have demonstrated that antibodies targeting SslE can neutralize its enzymatic activity and reduce bacterial colonization in vivo (Nesta et al., 2014). The protein's role in pathogenesis and its presence in both enteric and extraintestinal strains highlight its potential as a multi-purpose therapeutic target for anti-virulence strategies.

Other names

YghJAccessory colonization proteinAcpM60-like metalloproteaseLipoprotein YghJ

Neutralization of mucinase activity and inhibition of bacterial colonization through antibody binding