3J93

Fitting of Fab into the cryoEM density map of EV71 procapsid in complex with Fab22A12

Summary for 3J93

• Entry DOI: 10.2210/pdb3j93/pdb
• Related: 3J91
• EMDB information: 6200
• Descriptor: neutralizing antibody 22A12, light chain, neutralizing antibody 22A12, heavy chain (2 entities in total)
• Functional Keywords: fab, ev71, fab22a12, immune system
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 2
• Total formula weight: 46610.88

Authors

Shingler, K.L.,Cifuente, J.O.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Hafenstein, S. (deposition date: 2014-12-02, release date: 2014-12-24, Last modification date: 2024-11-06)

Primary citation

Shingler, K.L.,Cifuente, J.O.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Hafenstein, S.
The enterovirus 71 procapsid binds neutralizing antibodies and rescues virus infection in vitro.
J.Virol., 89:1900-1908, 2015

PubMed Abstract: Enterovirus 71 (EV71) is responsible for seasonal outbreaks of hand, foot, and mouth disease in the Asia-Pacific region. The virus has the capability to cause severe disease and death, especially in young children. Although several vaccines are currently in clinical trials, no vaccines or therapeutics have been approved for use. Previous structural studies have revealed that two antigenically distinct capsid forms are produced in EV71-infected cells: an expanded empty capsid, sometimes called a procapsid, and the infectious virus. Specifically, an immunodominant epitope of EV71 that maps to the virus canyon is structurally different in the procapsid and virus. This structure-function study shows that the procapsid can sequester antibodies, thus enhancing EV71 infection in vitro. The results presented here suggest that, due to conformational differences between the EV71 procapsid and virus, the presence of the procapsid in natural virus infections should be considered in the future design of vaccines or therapeutics.

PubMed: 25428877
DOI: 10.1128/JVI.03098-14

Experimental method

ELECTRON MICROSCOPY (8.8 Å)