title: Meningococcal ligands and molecular targets of the host.
abstract: Meningococcal mechanisms of adhesion are complex, involving multiple adhesins and their respective target receptors on host cells. Three major surface structures--pili, Opa, and Opc--have been known for some time to mediate meningococcal adhesion to target human cells. More recently, several other relatively minor adhesins have also come to light. The literature on bacterial adhesion mechanisms provides numerous examples of various adhesins acting cooperatively in an apparently hierarchical and sequential manner; in other instances, adhesins may act in concert leading to high avidity interactions, often a prelude to cellular invasion and tissue penetration. Such examples are also present in the case of meningococci, although our knowledge of adhesin cooperation and synergy is far from complete. Meningococcal mechanisms used to target the host, which are often specific for the host or a tissue within the host, include both lectin-like interactions and protein-protein interactions; the latter tend to determine specificity in general. Understanding (a) what determines specificity (i.e. molecular features of adhesins and receptors), (b) encourages cellular penetration (i.e. adhesin pairs, which act in concert or synergistically to deliver effective signals for invasion and induce other cellular responses), (c) level of redundancy (more than one mechanisms of targeting host receptors), (d) host situations that encourage tissue penetration (inflammatory situations during which circulating cytokines upregulate target cell receptors, effectively encouraging greater adhesion/invasion), and (e) down-stream effects on host functions in general are all clearly important in our future strategies of controlling meningococcal pathogenesis.
authors: School of Cellular and Molecular Medicine, University of Bristol, Bristol, UK.
authors: Darryl J
authors: DJ
authors: Hill
authors: Mumtaz
authors: M
authors: Virji
mesh_terms: D018829:Adhesins, Bacterial / Q000378:metabolism*; D001422:Bacterial Adhesion / Q000502:physiology*; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D010861:Fimbriae, Bacterial / Q000378:metabolism; D054884:Host-Pathogen Interactions; D006801:Humans; D009345:Neisseria meningitidis / Q000378:metabolism* / Q000502:physiology; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000378:metabolism*; D051193:Toll-Like Receptors / Q000378:metabolism
chemical_list: D018829:Adhesins, Bacterial; D015815:Cell Adhesion Molecules; D011956:Receptors, Cell Surface; D051193:Toll-Like Receptors