title: The I22V and L72S substitutions in West Nile virus prM protein promote enhanced prM/E heterodimerisation and nucleocapsid incorporation.
abstract: BACKGROUND
  Amino acid substitutions I22V and L72S in the prM protein of West Nile virus Kunjin strain (WNVKUN) were previously shown to enhance virus secretion and virulence, but a mechanism by which this occurred was not determined.
  
  
  RESULTS
  Using pulse-chase experiments followed by co-immunoprecipitation with anti-E antibody, we demonstrated that the I22V and L72S substitutions enhanced prM/E heterodimerization for both the E-glycosylated and E-unglycosylated virus. Furthermore, analysis of secreted particles revealed that I22V and L72S substitutions also enhanced nucleocapsid incorporation.
  
  
  CONCLUSIONS
  We have demonstrated mechanistically that improved secretion of virus particles in the presence of I22V and L72S substitutions was contributed by more efficient prM/E heterodimerization.
authors.affiliation: Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, 4072, Australia. y.setoh@uq.edu.au.
authors.forename: Yin Xiang
authors.initials: YX
authors.lastname: Setoh
authors.affiliation: Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, 4072, Australia. s.tan5@uq.edu.au.|Present Address: Sir Albert Sakzewski Virus Research Centre, Clinical Medical Virology Centre, Herston, QLD, Australia. s.tan5@uq.edu.au.
authors.forename: Cindy Si En
authors.initials: CS
authors.lastname: Tan
authors.affiliation: Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, 4072, Australia. Natalie.Prow@qimrberghofer.edu.au.|Present Address: QIMR Berghofer Medical Research Institute, Brisbane, QLD, Australia. Natalie.Prow@qimrberghofer.edu.au.
authors.forename: Natalie A
authors.initials: NA
authors.lastname: Prow
authors.affiliation: Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, 4072, Australia. j.peters2@uq.edu.au.
authors.forename: Jody
authors.initials: J
authors.lastname: Hobson-Peters
authors.affiliation: Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, 4072, Australia. p.young@uq.edu.au.
authors.forename: Paul R
authors.initials: PR
authors.lastname: Young
authors.affiliation: Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, 4072, Australia. alexander.khromykh@uq.edu.au.
authors.forename: Alexander A
authors.initials: AA
authors.lastname: Khromykh
authors.affiliation: Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, QLD, 4072, Australia. roy.hall@uq.edu.au.
authors.forename: Roy A
authors.initials: RA
authors.lastname: Hall
mesh_terms: D019943:Amino Acid Substitution; D000818:Animals; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D055503:Protein Multimerization; D014759:Viral Envelope Proteins / Q000235:genetics* / Q000378:metabolism*; D057074:Virus Release; D014902:West Nile virus / Q000235:genetics / Q000502:physiology*
chemical_list: D050505:Mutant Proteins; D014759:Viral Envelope Proteins; C074932:prM protein, Flavivirus; C065696:glycoprotein E, Flavivirus