Mucin-degrading metalloprotease YghJ (SslE) (YghJ)

YghJ, also known as SslE, is a highly conserved, secreted, and surface-localized lipoprotein found in various pathogenic strains of Escherichia coli, including Enterotoxigenic E. coli (ETEC) and Extraintestinal pathogenic E. coli (ExPEC) [1, 5]. It functions as a zinc-metalloprotease with an M60-like domain that specifically targets and degrades host mucins, such as MUC2 and MUC3, which are critical components of the protective mucus layer on mucosal surfaces [3, 5]. By breaking down this barrier, YghJ facilitates bacterial access to the underlying epithelium, promoting colonization, biofilm formation, and the delivery of other toxins like heat-labile toxin (LT) [5, 10]. Beyond its role in colonization, YghJ acts as a proinflammatory stimulus by serving as a Toll-like receptor 2 (TLR2) agonist, triggering the release of cytokines and contributing to the pathogenesis of sepsis and neonatal meningitis [7, 9]. The protein is also involved in the induction of hemorrhagic fluid accumulation and tissue damage in the intestine [1, 8]. Due to its broad conservation across diverse E. coli pathotypes and its essential role in virulence, YghJ is a prominent candidate for the development of broadly protective vaccines [4, 12]. Current research focuses on utilizing recombinant YghJ/SslE as a vaccine antigen to elicit neutralizing antibodies that prevent bacterial adhesion and infection [6, 13]. Therapeutic strategies targeting YghJ aim to neutralize its mucinase activity, thereby maintaining the integrity of the host's mucosal barrier [3, 12].

Other names

SslESecreted surface-localized effectorECO-005Mucinase YghJECOK1-3385

Neutralization of mucinase activity and prevention of bacterial adhesion to host epithelial cells via antibody-mediated inhibition.