Adenovirus fiber knob protein

The **Adenovirus fiber knob protein** is a structural viral protein that forms the terminal domain ("knob") of the trimeric fiber projecting from each vertex of the adenovirus capsid[1][2][3]. This knob is responsible for binding to cellular receptors, most notably the coxsackievirus and adenovirus receptor (CAR) in many adenovirus species, and to alternative receptors such as CD46 (for group B adenoviruses) and sialic acid-containing glycans (for some species D serotypes)[1][2][4][5]. The diversity and structural variation in the fiber-knob domain among adenovirus serotypes determines host cell specificity and tissue tropism, impacting both infection and the targeting profile of adenoviral vectors used in gene therapy and vaccine delivery[1][2]. The fiber-knob engages host receptors through well-characterized loops, and its interaction with CAR is critical for viral entry in many serotypes, although affinity and primary receptor usage can vary[1][2]. While not a conventional therapeutic target, this protein is of high biomedical interest as a determinant of viral pathogenicity, vector tropism, and immunogenicity, with direct implications for the design of viral vectors for vaccines and gene therapies[1][2][3].

Other names

Adenovirus fiber proteinAdenovirus fiber-knobFiber-knobAdenovirus attachment proteinAdenoviral fiber knob