Reduced cellular binding affinity has profoundly different impacts on the spread of distinct poxviruses.

ABSTRACT: Poxviruses are large enveloped viruses that replicate exclusively in the cytoplasm. Like all viruses, their replication cycle begins with virion adsorption to the cell surface. Unlike most other viral families, however, no unique poxviral receptor has ever been identified. In the absence of a unique receptor, poxviruses are instead thought to adhere to the cell surface primarily through electrostatic interactions between the positively charged viral envelope proteins and the negatively charged sulfate groups on cellular glycosaminoglycans (GAGs). While these negatively charged GAGs are an integral part of all eukaryotic membranes, their specific expression and sulfation patterns differ between cell types. Critically, while poxviral binding has been extensively studied using virally centere

SUBMITTER: Flores EB 

PROVIDER: S-EPMC7192435 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature