Integrins alphavbeta3 and alphavbeta5 promote adenovirus internalization but not virus attachment
Article Abstract:
Adenoviruses attach to cells via a 186-kd fiber protein and a 400-kd penton base that contains five Arg-Gly-Asp sequences. The Arg-Gly-Asp sequence mediates cell adhesion through heterodimeric cell surface receptors called integrins. A study was conducted to differentiate the process of viral attachment from subsequent internalization. Results showed that antibodies against vitronectin-binding integrins alphavbeta3 and alphavbeta5 prevent virus internalization without affecting attachment. Thus, integrins alphavbeta3 and alphavbeta5 promote adenovirus internalization.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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Role of alpha v integrins in adenovirus cell entry and gene delivery
Article Abstract:
A study has been conducted to discuss the earliest interactions of the adenovirus with its cellular receptors and to investigate the role of the virus internalization receptors, integrins alpha v beta 3 and alpha v beta 5. Integrins have been known to promote adenovirus entry both in vitro and in vivo environments. Findings have indicated that while integrins are required for virus penetration, they are necessarily sufficient. Some other elements may have to be present to complete the invasion process.
Publication Name: Microbiology and Molecular Biology Reviews
Subject: Biological sciences
ISSN: 1092-2172
Year: 1999
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Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity
Article Abstract:
Research was conducted to study the disruption of angiogenesis by a fragment of matrix metalloproteinase 2 (MMP-2) called PEX. Fusion proteins were prepared using primers based on the avian MMP-2 sequence. Results indicated that MMP-2 localizes in a proteolytically active form on the surface of invasive cells based on its ability to bind integrin alpha-v-beta-3. They also showed that PEX blocks MMP-2 binding to alpha-V-beta3, resulting in a loss of cell-associated collagenolytic activity.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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