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Is the Glycoprotein Responsible for the Differences in Dispersal Rates between Lettuce Necrotic Yellows Virus Subgroups?
Prabowo, Eko Y; Valmonte-Cortes, Gardette R; Darling, Toni Louise; Buckley, Elizabeth; Duxbury, Mark; Seale, Brent; Higgins, Colleen M.
Afiliação
  • Prabowo EY; School of Science, Auckland University of Technology, Auckland 1010, New Zealand.
  • Valmonte-Cortes GR; Department of Microbiology and Molecular Biology Testing of Drugs and Food, The National Agency of Drug and Food Control, Jakarta 10560, Indonesia.
  • Darling TL; School of Science, Auckland University of Technology, Auckland 1010, New Zealand.
  • Buckley E; School of Science, Auckland University of Technology, Auckland 1010, New Zealand.
  • Duxbury M; School of Science, Auckland University of Technology, Auckland 1010, New Zealand.
  • Seale B; School of Science, Auckland University of Technology, Auckland 1010, New Zealand.
  • Higgins CM; School of Science, Auckland University of Technology, Auckland 1010, New Zealand.
Viruses ; 14(7)2022 07 20.
Article em En | MEDLINE | ID: mdl-35891554
ABSTRACT
Lettuce necrotic yellows virus is a type of species in the Cytorhabdovirus genus and appears to be endemic to Australia and Aotearoa New Zealand (NZ). The population of lettuce necrotic yellows virus (LNYV) is made up of two subgroups, SI and SII. Previous studies demonstrated that SII appears to be outcompeting SI and suggested that SII may have greater vector transmission efficiency and/or higher replication rate in its host plant or insect vector. Rhabdovirus glycoproteins are important for virus-insect interactions. Here, we present an analysis of LNYV glycoprotein sequences to identify key features and variations that may cause SII to interact with its aphid vector with greater efficiency than SI. Phylogenetic analysis of glycoprotein sequences from NZ isolates confirmed the existence of two subgroups within the NZ LNYV population, while predicted 3D structures revealed the LNYV glycoproteins have domain architectures similar to Vesicular Stomatitis Virus (VSV). Importantly, changing amino acids at positions 244 and 247 of the post-fusion form of the LNYV glycoprotein altered the predicted structure of Domain III, glycosylation at N248 and the overall stability of the protein. These data support the glycoprotein as having a role in the population differences of LNYV observed between Australia and New Zealand.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Rhabdoviridae / Proteínas Virais Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Rhabdoviridae / Proteínas Virais Idioma: En Ano de publicação: 2022 Tipo de documento: Article