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-Structure paper
タイトル | Structural comparison of four different antibodies interacting with human papillomavirus 16 and mechanisms of neutralization. |
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ジャーナル・号・ページ | Virology, Vol. 483, Page 253-263, Year 2015 |
掲載日 | 2015年5月19日 |
著者 | Jian Guan / Stephanie M Bywaters / Sarah A Brendle / Hyunwook Lee / Robert E Ashley / Alexander M Makhov / James F Conway / Neil D Christensen / Susan Hafenstein / |
PubMed 要旨 | Cryo-electron microscopy (cryo-EM) was used to solve the structures of human papillomavirus type 16 (HPV16) complexed with fragments of antibody (Fab) from three different neutralizing monoclonals ...Cryo-electron microscopy (cryo-EM) was used to solve the structures of human papillomavirus type 16 (HPV16) complexed with fragments of antibody (Fab) from three different neutralizing monoclonals (mAbs): H16.1A, H16.14J, and H263.A2. The structure-function analysis revealed predominantly monovalent binding of each Fab with capsid interactions that involved multiple loops from symmetry related copies of the major capsid protein. The residues identified in each Fab-virus interface map to a conformational groove on the surface of the capsomer. In addition to the known involvement of the FG and HI loops, the DE loop was also found to constitute the core of each epitope. Surprisingly, the epitope mapping also identified minor contributions by EF and BC loops. Complementary immunological assays included mAb and Fab neutralization. The specific binding characteristics of mAbs correlated with different neutralizing behaviors in pre- and post-attachment neutralization assays. |
リンク | Virology / PubMed:25996608 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 13.0 - 14.0 Å |
構造データ | EMDB-5990: Electron cryo-microscopy of quasi-human papillomavirus 16 complexed with Fab H16.1A |
由来 |
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キーワード | VIRUS/IMMUNE SYSTEM / L1 pentamer / quasi-HPV16 / L1 capsomer / Rosie online / VIRUS-IMMUNE SYSTEM complex |