3J8Z

Cryo-EM reconstruction of quasi-HPV16 complex with H16.1A Fab

Summary for 3J8Z

• Entry DOI: 10.2210/pdb3j8z/pdb
• Related: 3J8V 3J8W
• EMDB information: 5990 6121 6184
• Descriptor: L1, H16.1A light chain, H16.1A heavy chain (3 entities in total)
• Functional Keywords: l1 pentamer, quasi-hpv16, l1 capsomer, rosie online, virus-immune system complex, virus/immune system
• Biological source: Human papillomavirus type 16; More
• Total number of polymer chains: 13
• Total formula weight: 355331.40

Authors

Guan, J.,Hafenstein, S. (deposition date: 2014-11-20, release date: 2015-05-06, Last modification date: 2018-07-18)

Primary citation

Guan, J.,Bywaters, S.M.,Brendle, S.A.,Lee, H.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Christensen, N.D.,Hafenstein, S.
Structural comparison of four different antibodies interacting with human papillomavirus 16 and mechanisms of neutralization.
Virology, 483:253-263, 2015

PubMed Abstract: 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.

PubMed: 25996608
DOI: 10.1016/j.virol.2015.04.016

Experimental method

ELECTRON MICROSCOPY (14 Å)