Secreted sticky lipoprotein (SslE) (SslE)

Secreted sticky lipoprotein (SslE), historically referred to as YghJ, is a highly conserved surface-exposed lipoprotein and zinc-metallopeptidase secreted by various pathogenic strains of Escherichia coli, including Enterotoxigenic (ETEC) and Extraintestinal pathogenic E. coli (ExPEC) [1, 2]. It serves as a critical virulence factor by functioning as a mucinase that degrades major human intestinal mucins, such as MUC2 and MUC3, thereby facilitating bacterial transit through the protective mucus barrier to reach the underlying host epithelium [3, 4]. Beyond its enzymatic role, SslE contributes to bacterial aggregation and biofilm formation, which are essential for stable colonization and persistence within the host environment [2, 5]. Due to its broad conservation across diverse E. coli pathotypes and its accessibility on the bacterial surface, SslE is a primary target for the development of broad-spectrum vaccines and therapeutic antibodies [1, 6]. Experimental studies have demonstrated that antibodies targeting SslE can neutralize its mucinase activity and significantly reduce bacterial colonization in vivo, making it a promising candidate for preventing both enteric and extraintestinal infections [5, 6]. [1] UniProt Consortium, P0ADK8; [2] Moriel et al. (2010) PNAS; [3] Luo et al. (2014) Infection and Immunity; [4] Fleckenstein et al. (2014) Microbes and Infection; [5] Nesta et al. (2014) PLOS Pathogens; [6] Valeri et al. (2015) EMBO Reports.

Other names

YghJMucin-degrading metalloprotease YghJECOPEscherichia coli opportunistic pathogen protein

Neutralization of mucinase activity to prevent bacterial penetration of the host mucus layer and subsequent attachment to epithelial cells.