Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10

AbstractCoxsackievirus A10 (CV-A10) is responsible for an escalating number of severe infections in children, but no prophylactics or therapeutics are currently available. KREMEN1 (KRM1) is the entry receptor for the largest receptor-group of hand-foot-and-mouth disease causing viruses, which includes CV-A10. We report here structures of CV-A10 mature virus alone and in complex with KRM1 as well as of the CV-A10 A-particle. The receptor spans the viral canyon with a large footprint on the virus surface. The footprint has some overlap with that seen for the neonatal Fc receptor complexed with enterovirus E6 but is larger and distinct from that of another enterovirus receptor SCARB2. Reduced occupancy of a particle-stabilising pocket factor in the complexed virus and the presence of both unbound and expanded virus particles suggests receptor binding initiates a cascade of conformational changes that produces expanded particles primed for viral uncoating.

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Foot-and-mouth disease virus particles inactivated with binary ethylenimine are efficiently internalized into cultured cells

Vaccine ◽

10.1016/j.vaccine.2011.10.031 ◽

2011 ◽

Vol 29 (52) ◽

pp. 9655-9662 ◽

Cited By ~ 8

Author(s):

Miguel A. Martín-Acebes ◽

Ángela Vázquez-Calvo ◽

Mónica González-Magaldi ◽

Francisco Sobrino

Keyword(s):

Disease Virus ◽

Cultured Cells ◽

Foot And Mouth Disease ◽

Mouth Disease ◽

Virus Particles ◽

Mouth Disease Virus ◽

Foot And Mouth

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Research on Measures of Reducing Environmental Pollutions by Empty Capsid Virus Particles with Vaccine of Foot and Mouth Disease Virus to Control FMD

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.1023.257 ◽

2014 ◽

Vol 1023 ◽

pp. 257-261

Author(s):

Qi Hong ◽

Zi Hong Liu ◽

Duan Dan Han

Keyword(s):

Virus Particle ◽

Foot And Mouth Disease ◽

Mouth Disease ◽

Promising Candidate ◽

Effective Measure ◽

Virus Particles ◽

Empty Capsid ◽

Mouth Disease Virus ◽

Foot And Mouth ◽

Potential Benefits

Foot-and-mouth disease (FMD) is a highly contagious disease in cloven-hoofed animals, and had been broken out worldwide several times in recent years. In order to extinct outbreak of FMD, a large number of infected animals are slaughtered in some countries, and the slaughterings had been caused a series of environmental pollutions seriously. To reduce this kind of pollution, vaccination is an effective measure to protect animals against FMD, however, FMD virus (FMDV) escaping from manufacturing plant and inactivated incompletely during vaccine production could cause an outbreak of FMD. Therefore, inactivated FMDV vaccines are not safe to animals and environment. FMDV empty capsid (lacking nucleic acid) can elicit the same antibody response as infectious FMDV, thus, empty capsid virus particle vaccine of FMDV would be the most promising candidate vaccine for its safety and protection against FMDV. In this report, we studied the empty capsid virus particle vaccine of FMDV to control FMD and its potential benefits to the environment.

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Sequence adaptations affecting cleavage of the VP1/2A junction by the 3C protease in foot-and-mouth disease virus-infected cells

Journal of General Virology ◽

10.1099/vir.0.068197-0 ◽

2014 ◽

Vol 95 (11) ◽

pp. 2402-2410 ◽

Cited By ~ 10

Author(s):

Maria Gullberg ◽

Charlotta Polacek ◽

Graham J. Belsham

Keyword(s):

Disease Virus ◽

Foot And Mouth Disease ◽

Mouth Disease ◽

Single Amino Acid ◽

Virus Particles ◽

3C Protease ◽

Serotype O ◽

Single Amino Acid Residue ◽

Mouth Disease Virus ◽

Foot And Mouth

The foot-and-mouth disease virus (FMDV) capsid protein precursor P1-2A is cleaved by the virus-encoded 3C protease to VP0, VP3, VP1 and 2A. It was shown previously that modification of a single amino acid residue (K210E) within the VP1 protein and close to the VP1/2A cleavage site, inhibited cleavage of this junction and produced ‘self-tagged’ virus particles. A second site substitution (E83K) within VP1 was also observed within the rescued virus [Gullberg et al. (2013). J Virol 87, 11591–11603]. It was shown here that introduction of this E83K change alone into a serotype O virus resulted in the rapid accumulation of a second site substitution within the 2A sequence (L2P), which also blocked VP1/2A cleavage. This suggests a linkage between the E83K change in VP1 and cleavage of the VP1/2A junction. Cells infected with viruses containing the VP1 K210E or the 2A L2P substitutions contained the uncleaved VP1-2A protein. The 2A L2P substitution resulted in the VP1/2A junction being highly resistant to cleavage by the 3C protease, hence it may be a preferred route for ‘tagging’ virus particles.

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