Cellular interactions by LPxTG-anchored pneumococcal adhesins and their streptococcal homologues

Abstract

In this review we focus on three important families of LPxTG-anchored adhesins in the human pathogen Streptococcus pneumoniae, but also their homologues in related streptococci. We discuss the contribution of these streptococcal adhesins to host tropism, pathogenesis and their interactions with different host cell types. The first surface structures discussed are the heteropolymeric pili that have been found in important streptococcal pathogens such as S. pneumoniae, S. pyogenes, S. agalactiae and E. faecalis/faecium. Major and minor pilus subunit proteins are covalently joined and finally attached to the cell wall through the action of specific sortases. The role of pili and individual pilin subunits in adhesion and pathogenesis and their structure and assembly in different streptococcal species are being covered. Furthermore, we address recent findings regarding a family of large glycosylated serine-rich repeat (SRR) proteins that act as fibrillar adhesins for which homologues have been found in several streptococcal species including pneumococci. In the pneumococcal genome both pili and its giant SRR protein are encoded by accessory genes present in particular clonal lineages for which epidemiological information is available. Finally, we briefly discuss the role played by the pneumococcal neuraminidase NanA in adhesion and pathogenesis.