ArticleActa crystallographica. Section D, Biological crystallography2014
Structure of the virulence-associated protein VapD from the intracellular pathogen Rhodococcus equi.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Phenotypical and molecular characterization of Rhodococcus equi isolated from foals in the Agreste region of Pernambuco - Brazil.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025Article
- Pathotyping and molecular serotyping of clinical isolates of Glaesserella parasuis in Taiwan.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025Article
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- Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB.Acta crystallographica. Section F, Structural biology communications · 2021Article
- The pathogenic actinobacterium Rhodococcus equi: what's in a name?Molecular microbiology · 2019Review
- VapA of Rhodococcus equi binds phosphatidic acid.Molecular microbiology · 2018Article
- Identification of a VapA virulence factor functional homolog in Rhodococcus equi isolates housing the pVAPB plasmid.PloS one · 2018Article
- The Rhodococcus equi virulence protein VapA disrupts endolysosome function and stimulates lysosome biogenesis.MicrobiologyOpen · 2017Article
- Novel Moraxella catarrhalis prophages display hyperconserved non-structural genes despite their genomic diversity.BMC genomics · 2015Article
- Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi.Veterinary microbiology · 2015Article
- Transcriptome reprogramming by plasmid-encoded transcriptional regulators is required for host niche adaption of a macrophage pathogen.Infection and immunity · 2015Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Rhodococcus equi is a multi-host pathogen that infects a range of animals as well as immune-compromised humans. Equine and porcine isolates harbour a virulence plasmid encoding a homologous family of virulence-associated proteins associated with the capacity of R. equi to divert the normal processes of endosomal maturation, enabling bacterial survival and proliferation in alveolar macrophages. To provide a basis for probing the function of the Vap proteins in virulence, the crystal structure of VapD was determined. VapD is a monomer as determined by multi-angle laser light scattering. The structure reveals an elliptical, compact eight-stranded β-barrel with a novel strand topology and pseudo-twofold symmetry, suggesting evolution from an ancestral dimer. Surface-associated octyl-β-D-glucoside molecules may provide clues to function. Circular-dichroism spectroscopic analysis suggests that the β-barrel structure is preceded by a natively disordered region at the N-terminus. Sequence comparisons indicate that the core folds of the other plasmid-encoded virulence-associated proteins from R. equi strains are similar to that of VapD. It is further shown that sequences encoding putative R. equi Vap-like proteins occur in diverse bacterial species. Finally, the functional implications of the structure are discussed in the light of the unique structural features of VapD and its partial structural similarity to other β-barrel proteins.
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