Three-dimensional structure of foot-and-mouth disease virus and its biological functions

Han, Shuang; Guo, Huichen; Sun, Shiqi

doi:10.1007/s00705-014-2278-x

Cited by 36 publications

(42 citation statements)

References 149 publications

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“…Subtle, rather than large, conformational change is reminiscent of the crystal structures of foot-and-mouth disease viruses (FMDVs) complexed with heparinoid oligosaccharides 45, 46, 47. So too are pre-formed sulfate-binding sites containing arginines, and natural or in vitro modulation of binding affinity and infectivity upon mutation of these residues 13, 46.…”

Section: Discussionmentioning

confidence: 99%

The 2.8 Å Electron Microscopy Structure of Adeno-Associated Virus-DJ Bound by a Heparinoid Pentasaccharide

Xie

Spear

Noble

et al. 2017

Molecular Therapy - Methods & Clinical Development

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Atomic structures of adeno-associated virus (AAV)-DJ, alone and in complex with fondaparinux, have been determined by cryoelectron microscopy at 3 Å resolution. The gene therapy vector, AAV-DJ, is a hybrid of natural serotypes that was previously derived by directed evolution, selecting for hepatocyte entry and resistance to neutralization by human serum. The structure of AAV-DJ differs from that of parental serotypes in two regions where neutralizing antibodies bind, so immune escape appears to have been the primary driver of AAV-DJ’s directed evolution. Fondaparinux is an analog of cell surface heparan sulfate to which several AAVs bind during entry. Fondaparinux interacts with viral arginines at a known heparin binding site, without the large conformational changes whose presence was controversial in low-resolution imaging of AAV2-heparin complexes. The glycan density suggests multi-modal binding that could accommodate sequence variation and multivalent binding along a glycan polymer, consistent with a role in attachment, prior to more specific interactions with a receptor protein mediating entry.

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Section: Discussionmentioning

confidence: 99%

The 2.8 Å Electron Microscopy Structure of Adeno-Associated Virus-DJ Bound by a Heparinoid Pentasaccharide

Xie

Spear

Noble

et al. 2017

Molecular Therapy - Methods & Clinical Development

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“…The viral particle is a spherical icosahedron with a diameter of approximately 25 to 30 nm and no lipid envelope. The surface of the virion is smooth, unusual among picornaviruses [40,41]. Four proteins, namely virus protein (VP) 1 (1D), VP2 (1B), VP3 (1C), and VP4 (1A), form the viral capsid.…”

Section: Virion Structurementioning

confidence: 99%

“…Each of the surface-exposed VPs is formed by a betasandwich consisting of eight single strands labeled B, I, D, G, C, H, E, and F and seven connecting loops that are named after the adjacent beta-strands [43]. While the BIDG lamella is drawn together in the inner capsid, the CHEF strands as well as the associated loops are exposed on the outer capsid surface [41]. To make up the viral capsid, heterooligomeric protomers are built from one copy of each structural protein originating from the same P1-2A precursor molecule.…”

Section: Virion Structurementioning

confidence: 99%

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Cell culture propagation of foot-and-mouth disease virus: adaptive amino acid substitutions in structural proteins and their functional implications

Dill

Eschbaumer

2019

Virus Genes

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Foot-and-mouth disease is endemic in livestock in large parts of Africa and Asia, where it is an important driver of food insecurity and a major obstacle to agricultural development and the international trade in animal products. Virtually all commercially available vaccines are inactivated whole-virus vaccines produced in cell culture, but the adaptation of a field isolate of the virus to growth in culture is laborious and time-consuming. This is of particular concern for the development of vaccines to newly emerging virus lineages, where long lead times from virus isolate to vaccine can delay the implementation of effective control programs. High antigen yields in production cells are also necessary to make vaccines affordable for less developed countries in endemic areas. Therefore, a rational approach to cell culture adaptation that combines prior knowledge of common adaptive mutations and reverse genetics techniques is urgently required. This review provides an overview of amino acid exchanges in the viral capsid proteins in the context of adaptation to cell culture.

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“…The FMDV genome encodes a total of 12 mature proteins translated from a single polyprotein coding region approximately 7 kilobases in length. The structural proteins VP1, VP2, VP3, and VP4 compose the capsid, with all but VP4 serving as major antigenic targets and taking part in receptor-mediated host cell entry [4, 6]. Positive selection has been identified predominantly within the capsid-encoding segments, leading to elevated amino acid replacement rates [7–9].…”

Section: Introductionmentioning

confidence: 99%

The evolution of a super-swarm of foot-and-mouth disease virus in cattle

Arzt

Fish

Pauszek

et al. 2019

Preprint

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23 Foot-and-mouth disease (FMD) is a highly contagious viral disease that severely impacts global 24 food security and is one of the greatest constraints on international trade of animal products.25 Extensive viral population diversity and rapid, continuous mutation of circulating FMD viruses 26 (FMDVs) pose significant obstacles to the control and ultimate eradication of this important 27 transboundary pathogen. The current study investigated mechanisms contributing to within-host 28 evolution of FMDV in a natural host species (cattle). Specifically, vaccinated and non-29 vaccinated cattle were infected with FMDV under controlled, experimental conditions and 30 subsequently sampled for up to 35 days to monitor viral genomic changes as related to phases of 31 disease and experimental cohorts. Consensus-level genomic changes across the entire FMDV 32 coding region were characterized through three previously defined stages of infection: early, 33 transitional, and persistent. The overall conclusion was that viral evolution occurred via a 34 combination of two mechanisms: emergence of full-genomic minority haplotypes from within 35 the inoculum super-swarm, and concurrent continuous point mutations. Phylogenetic analysis 36 indicated that individuals were infected with multiple distinct haplogroups that were pre-existent 37 within the ancestral inoculum used to infect all animals. Multiple shifts of dominant viral 38 haplotype took place during the early and transitional phases of infection, whereas few shifts 39 occurred during persistent infection. These insights into FMDV population dynamics have 40 important implications for virus sampling methodology and molecular epidemiology. 41 42 43 3 44 Introduction 45Foot-and-mouth disease (FMD) is a highly contagious viral disease that affects wild and 46 domestic even-toed ruminants [1, 2]. FMD is a major global concern for livestock owners and 47 managers, and the disease has substantial impact on regulation of international trade in animal 48 products [3]. The classical signs of disease include oral and pedal vesicles and erosions, often 49 associated with lameness, pyrexia, and obtundation [2, 4]. The causative agent, FMD virus 50 (FMDV) is extremely contagious and disseminates rapidly amongst susceptible animals. 51 Although the disease is rarely fatal, FMD-endemic regions incur substantial economic burdens 52 associated with production losses and disease control [5]. Sporadic outbreaks in countries that 53 are normally free from FMD result in costly mediations including culling of large numbers of 54 animals and animal movement restrictions, as well as massive economic losses due to 55 implications on trade in animal products. 56 FMDV (family: Picornaviridae, genus: Aphthovirus) is a single-stranded RNA virus which 57 exists in 7 defined serotypes; O, A, C, Asia-1, and Southern African Territories (SAT) 1-3. The 58 FMDV genome encodes a total of 12 mature proteins translated from a single polyprotein coding 59 region approximately 7 kilobases in length. The structu...

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Three-dimensional structure of foot-and-mouth disease virus and its biological functions

Cited by 36 publications

References 149 publications

The 2.8 Å Electron Microscopy Structure of Adeno-Associated Virus-DJ Bound by a Heparinoid Pentasaccharide

The 2.8 Å Electron Microscopy Structure of Adeno-Associated Virus-DJ Bound by a Heparinoid Pentasaccharide

Cell culture propagation of foot-and-mouth disease virus: adaptive amino acid substitutions in structural proteins and their functional implications

The evolution of a super-swarm of foot-and-mouth disease virus in cattle

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