Source: http://www.asmscience.org/content/book/10.1128/9781555816698.ch05
Timestamp: 2019-04-21 08:40:37+00:00

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Clathrin is critical for internalization of many viruses, yet no one would consider it a receptor; similarly, although encephalomyocarditis virus binds to glycophorin A on nonpermissive red blood cells, glycophorin is not expressed on most permissive cell lines and is unlikely to be the real receptor. The author suggests that a putative receptor molecule should fulfill two general criteria. First, the molecule must interact with virus at the cell surface. Second, interaction with the molecule must promote infection. The typical picornavirus capsid is an icosahedral structure constructed of 12 pentamers, with each pentamer composed of five copies of each of the four viral structural proteins, VP1 to -4. The first and simplest function of a receptor is to permit virus attachment and to concentrate the virus at the cell surface so that subsequent events in infection can occur. Unlike most enteroviruses, which have evolved to resist gastric acidity as they move through the enteric tract, foot-and-mouth disease virus (FMDV) and some rhinoviruses are destabilized by acid. Virus receptors may also transmit intracellular signals that are important for infection. The same surface loop that displays the RGD motif is also a major site recognized by neutralizing antibodies. Coxsackievirus and adenovirus receptor (CAR) functions in cell-cell adhesion, mediating both homotypic and heterotypic interactions. The murine CAR homolog is a functional coxsackie B viruses (CVB) receptor and is most likely responsible for the susceptibility of mice to CVB infection.
Diverse structures of picornavirus receptor molecules. Important structural features of each receptor are indicated, with asterisks marking sites of virus attachment. PVR, ICAM-1, and CAR are members of the Ig superfamily. The hepatitis A virus receptor TIM-1 is composed of a single Ig domain atop a series of mucin-like repeats. DAF is linked to the membrane by a glycolipid (gpi) anchor; enterovirus 70 binds specifically to the N-terminal SCR domain, but other picornaviruses interact primarily with other SCRs. VLA-2 and αvβ3 are integrins, which are heterodimers composed of α and β subunits: VLA-2 α includes an extra domain, the I-domain, which serves as the attachment site for EV1; αvβ3 recognizes viral RGD peptides, which are bound at the interface between the two subunits. Members of the LDLR family are characterized by cysteine-rich N-terminal repeats, which are recognized by minor group HRVs. PSGL-1 is a disulfide-linked heterodimer composed largely of mucin-like repeats; the projecting N-terminal peptide, which is characterized by sulfated tyrosine residues, is the attachment site for enterovirus 71. SCARB2 is a type III glycoprotein with two transmembrane segments; the structure of the virus-binding extracellular domain has not been determined.
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