Journal of Virology · 1994 · 194 citations · 18 references
Life SciencesBiochemistryMolecular BiologyMolecular VirologyProtein EngineeringVirologyViral AssemblyViral AttachmentViral InfectionsViral StructureViral TropismVirus StructureAdenoviral VectorsAdenovirus BiologyAmino AcidsHost Cell ReceptorsProteolytic ResistanceReceptorsViral Attachment ProteinsVirus Attachment Fibers
The adenovirus fiber appears as a long, thin projection terminated by a knob (head). The fiber consists of a trimeric protein whose head domain is thought to interact with cell receptors. The head part (amino acids 388 to 582) of adenovirus type 2 fiber was produced in a baculovirus expression system. The purified protein was shown to cross-link into trimers. It was very resistant to proteolytic attack and seemed to attain a high degree of compactness. The head domain efficiently inhibited attachment of adenovirus to receptors on the surface of HeLa cells, thereby confirming the hypothesis that the head domain interacts with viral receptors.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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Integrins αvβ3 and αvβ5 promote adenovirus internalization but not virus attachment
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