Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen (Nature, 2012, 485:256-259)

報告日期: 2012/10/23
報告時間: 15:10/16:00
報告學生: 王雅君
講評老師: 張志鵬
附件下載: 下載[1221-1348566647-1.pdf] 

Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen

Nature, 2012, 485, 256-259

Liya Hu, Sue E. Crawford, Rita Czako, Nicolas W. Cortes-Penfield, David F. Smith, Jacques Le Pendu, Mary K. Estes & B. V. Venkataram Prasad

Speaker: 王雅君                       日期: 2012/10/23

Commentator : 張志鵬老師                            時間: 15:10-1600                                       地點: 602教室

Abstract:

Rotavirusesinfection modulated by interaction with cell surface glycans causes of diseases in children range from acute gastroenteritis to lethal infection. Although the recognition of terminal or internal sialic acids have been investigated, the VP8* carbohydrate-recognizing domain of the outer capsid spike protein VP4, cloned from P[14] human rotavirus strain is not yet illuminated for cell attachment. Here, the authors expressed P[14]VP8* protein and analyzed the structural characteristics. The crystallography of P[14]VP8* showed a narrower cleft and some amino acids change which was not bound with sialic acid differed from other human strains. The authors also found that VP8* of strain P[14] specific bound to the A-type histo-blood group antigen(HBGA) by a high throughput screening of the glycan microarray. The binding of VP8* with A-type HBGA was then deciphered by co-crystallization. In addition, the interaction of P[14]VP8* with A-type HBGA were confirmed by using the inhibition of anti-A type antibody for P[14] virus infectivity in HT-29 cell and highly P[14] viral titer from CHO cell line transfected with A-type gene compared with parental cell. Because of mild amino acids change, the binding site of A-type HBGA was the same as sialic acid in VP8* structure of animal rotavirus strains. In conclusion, the authors demonstrated that A-type HBGA was an essential receptor for P[14] rotavirus strain in vitro and offer a helpful information to understand the interaction of human rotavirus and host cell for drug targets.