Mucin-degrading metalloprotease YghJ (YghJ)

Mucin-degrading metalloprotease YghJ, also known as SslE, is a large secreted lipoprotein and a critical virulence factor found in various pathogenic Escherichia coli strains, including Enterotoxigenic E. coli (ETEC) and Extraintestinal Pathogenic E. coli (ExPEC) (Luo et al., 2014, PMID: 24818661). It functions as a zinc-metalloprotease belonging to the M60-like family, specifically targeting and degrading host mucin glycoproteins (such as MUC2 and MUC3) that constitute the protective mucus barrier of the intestinal and extraintestinal tracts (Nesta et al., 2014, PMID: 24639449). By breaking down this barrier, YghJ facilitates bacterial penetration and subsequent adhesion to the underlying epithelial cells, which is essential for colonization and the delivery of toxins (Luo et al., 2014, PMID: 24818661). The protein undergoes O-linked glycosylation, a post-translational modification that may influence its stability and role as a surface-exposed antigen (UniProt, P0CK95). Due to its high conservation across diverse E. coli pathotypes and its indispensable role in infection, YghJ is a primary target for the development of broadly protective vaccines and therapeutic antibodies (Nesta et al., 2014, PMID: 24639449). Experimental studies have demonstrated that antibodies targeting YghJ can effectively neutralize its mucinase activity and reduce bacterial load in vivo (Fleckenstein et al., 2014, PMID: 24933307).

Other names

SslESecreted sticky lipoprotein EM60-like metalloproteaseECOP_03810AcpP-like protein

Neutralization of the protease activity to prevent the degradation of the host's protective mucus layer, thereby inhibiting bacterial access and adhesion to the underlying epithelial cells (Nesta et al., 2014, PMID: 24639449).