3J3Z

Structure of MA28-7 neutralizing antibody Fab fragment from electron cryo-microscopy of enterovirus 71 complexed with a Fab fragment

Summary for 3J3Z

• Entry DOI: 10.2210/pdb3j3z/pdb
• EMDB information: 5673
• Descriptor: MA28-7 neutralizing antibody light chain, MA28-7 neutralizing antibody heavy chain (2 entities in total)
• Functional Keywords: ev71, enterovirus, hfmd, strain-specific eptitope, vp1-145, immune system
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 2
• Total formula weight: 46610.88

Authors

Lee, H.,Cifuente, J.O.,Ashley, R.E.,Conway, J.F.,Makhov, A.M.,Tano, Y.,Shimizu, H.,Nishimura, Y.,Hafenstein, S. (deposition date: 2013-05-21, release date: 2013-08-28, Last modification date: 2024-11-27)

Primary citation

Lee, H.,Cifuente, J.O.,Ashley, R.E.,Conway, J.F.,Makhov, A.M.,Tano, Y.,Shimizu, H.,Nishimura, Y.,Hafenstein, S.
A strain-specific epitope of enterovirus 71 identified by cryo-electron microscopy of the complex with fab from neutralizing antibody.
J.Virol., 87:11363-11370, 2013

PubMed Abstract: Enterovirus 71 (EV71) is a picornavirus that causes outbreaks of hand, foot, and mouth disease (HFMD), primarily in the Asia-Pacific area. Unlike coxsackievirus A16, which also causes HFMD, EV71 induces severe neuropathology leading to high fatalities, especially among children under the age of 6 years. Currently, no established vaccines or treatments are available against EV71 infection. The monoclonal antibody MA28-7 neutralizes only specific strains of EV71 that have a conserved glycine at amino acid VP1-145, a surface-exposed residue that maps to the 5-fold vertex and that has been implicated in receptor binding. The cryo-electron microscopy structure of a complex between EV71 and the Fab fragment of MA28-7 shows that only one Fab fragment occupies each 5-fold vertex. A positively charged patch, which has also been implicated in receptor binding, lies within the Fab footprint. We identify the strain-specific epitope of EV71 and discuss the possible neutralization mechanisms of the antibody.

PubMed: 23946455
DOI: 10.1128/JVI.01926-13

Experimental method

ELECTRON MICROSCOPY (23.4 Å)