期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 106, 期 5, 页码 1566-1571出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0801433106
关键词
receptor; paramyxovirus; fusion protein; viral entry
资金
- Public Health Service [K08 AI56170, R21 AI073697, T32 AI007281, T32 AI007611, R01 AI32539]
- Elizabeth B. Lamb Center for Pediatric Research
- Vanderbilt-Ingram Cancer Center [P30 CA68485]
- Vanderbilt Digestive Disease Research Center [DK058404]
Human metapneumovirus (hMPV) is a recently described paramyxovirus that causes lower respiratory infections in children and adults worldwide. The hMPV fusion (F) protein is a membrane-anchored glycoprotein and major protective antigen. All hMPV F protein sequences determined to date contain an Arg-Gly-Asp (RGD) sequence, suggesting that F engages RGD-binding integrins to mediate cell entry. The divalent cation chelator EDTA, which disrupts heterodimeric integrin interactions, inhibits infectivity of hMPV but not the closely related respiratory syncytial virus (RSV), which lacks an RGD motif. Function-blocking antibodies specific for alpha v beta 1 integrin inhibit infectivity of hMPV but not RSV. Transfection of nonpermissive cells with alpha v or beta 1 cDNAs confers hMPV infectivity, whereas reduction of alpha v and beta 1 integrin expression by siRNA inhibits hMPV infection. Recombinant hMPV F protein binds to cells, whereas Arg-Gly-Glu (RGE)-mutant F protein does not. These data suggest that alpha v beta 1 integrin is a functional receptor for hMPV.
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