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Minimum determinants of transmissible gastroenteritis virus enteric tropism are located in the n-terminus of spike protein
Enteric tropism Recombinant virus Transmissible gastroenteritis virus Tropism amino acid sequence amino terminal sequence animal cell animal experiment article bacterial artificial chromosome binding site cell culture comparative study controlled study enteric virus gastrointestinal infection gene mutation genetic transfection glycosaminoglycan metabolism molecular cloning morbidity mortality nonhuman plasmid Porcine respiratory coronavirus protein motif protein stability protein structure respiratory virus reverse transcription polymerase chain reaction sequence analysis viral tropism virogenesis virus load virus recombinant virus release virus replication virus transmission chimeric antibody chimeric protein/ec [Endogenous Compound] complementary DNA glycosaminoglycan sialic acid unclassified drug virus RNA/ec [Endogenous Compound] virus spike protein/ec [Endogenous Compound] vitronectin engineered cell rs7 protein/ec [Endogenous Compound] sc11 protein/ec [Endogenous Compound] synaptic protein transport vesicle/ec [Endogenous Compound] ; 2020(Pathogens)
Article in English | January | ID: covidwho-830943
ABSTRACT
Transmissible gastroenteritis virus (TGEV) is an enteric coronavirus causing high morbidity and mortality in porcine herds worldwide, that possesses both enteric and respiratory tropism. The ability to replicate in the enteric tract directly correlates with virulence, as TGEVs with an exclusive respiratory tropism are attenuated. The tissue tropism is determined by spike (S) protein, although the molecular bases for enteric tropism remain to be fully characterized. Both pAPN and sialic acid binding domains (aa 506-655 and 145-155, respectively) are necessary but not sufficient for enteric tract infection. Using a TGEV infectious cDNA and enteric (TGEV-SC11) or respiratory (TGEV-SPTV) isolates, encoding a full-length S protein, a set of chimeric recombinant viruses, with a sequential modification in S protein amino terminus, was engineered. In vivo tropism, either enteric, respiratory or both, was studied by inoculating three-day-old piglets and analyzing viral titers in lung and gut. The data indicated that U655 G change in S gene (S219A in S protein) was required to confer enteric tropism to a respiratory virus that already contains the pAPN and sialic acid binding domains in its S protein. Moreover, an engineered virus containing U655 G and a 6 nt insertion at position 1124 (Y374-T375insND in S protein) was genetically stable after passage in cell cultures, and increased virus titers in gut by 1000-fold. We postulated that the effect of these residues in enteric tropism may be mediated by the modification of both glycosaminoglycan binding and S protein structure. Copyright © 2019 by the authors. Licensee MDPI, Basel, Switzerland.
Full text: Available Collection: Databases of international organizations Database: January Language: English Journal: Ec [Endogenous Compound] complementary DNA glycosaminoglycan sialic acid unclassified drug virus RNA Document Type: Article

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Full text: Available Collection: Databases of international organizations Database: January Language: English Journal: Ec [Endogenous Compound] complementary DNA glycosaminoglycan sialic acid unclassified drug virus RNA Document Type: Article