dc.contributor.author
Veit, Michael
dc.contributor.author
Gadalla, Mohamed Rasheed
dc.contributor.author
Zhang, Minze
dc.date.accessioned
2022-12-30T13:06:25Z
dc.date.available
2022-12-30T13:06:25Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/37375
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-37087
dc.description.abstract
Porcine reproductive and respiratory syndrome virus is a positive-stranded RNA virus of the family Arteriviridae. The Gp5/M dimer, the major component of the viral envelope, is required for virus budding and is an antibody target. We used alphafold2, an artificial-intelligence-based system, to predict a credible structure of Gp5/M. The short disulfide-linked ectodomains lie flat on the membrane, with the exception of the erected N-terminal helix of Gp5, which contains the antibody epitopes and a hypervariable region with a changing number of carbohydrates. The core of the dimer consists of six curved and tilted transmembrane helices, and three are from each protein. The third transmembrane regions extend into the cytoplasm as amphiphilic helices containing the acylation sites. The endodomains of Gp5 and M are composed of seven β-strands from each protein, which interact via β-strand seven. The area under the membrane forms an open cavity with a positive surface charge. The M and Orf3a proteins of coronaviruses have a similar structure, suggesting that all four proteins are derived from the same ancestral gene. Orf3a, like Gp5/M, is acylated at membrane-proximal cysteines. The role of Gp5/M during virus replication is discussed, in particular the mechanisms of virus budding and models of antibody-dependent virus neutralization.
en
dc.format.extent
34 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
porcine respiratory and reproductive syndrome virus
en
dc.subject.ddc
600 Technik, Medizin, angewandte Wissenschaften::610 Medizin und Gesundheit::616 Krankheiten
dc.subject.ddc
600 Technik, Medizin, angewandte Wissenschaften::610 Medizin und Gesundheit::615 Pharmakologie, Therapeutik
dc.title
Using Alphafold2 to Predict the Structure of the Gp5/M Dimer of Porcine Respiratory and Reproductive Syndrome Virus
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.articlenumber
13209
dcterms.bibliographicCitation.doi
10.3390/ijms232113209
dcterms.bibliographicCitation.journaltitle
International Journal of Molecular Sciences
dcterms.bibliographicCitation.number
21
dcterms.bibliographicCitation.originalpublishername
MDPI
dcterms.bibliographicCitation.volume
23
dcterms.bibliographicCitation.url
https://doi.org/10.3390/ijms232113209
refubium.affiliation
Veterinärmedizin
refubium.affiliation.other
Institut für Virologie
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
1422-0067