Both the P and V proteins of the porcine rubulavirus LPMV interact with the NP protein via their respective C-terminal unique parts

Virus Research

Volumn 83, Issue 1-2, 2002, Pages 31-41

  Svenda, Martin ^a,c   Hjertner, Bernt ^a,c   Linné, Tommy ^a   Berg, Mikael ^b  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b UPPSALA UNIVERSITY   (Sweden)

^c UPPSALA UNIVERSITY   (Sweden)

Author keywords

LPMV; Nucleocapsid; Nucleoprotein; Phosphoprotein; Porcine rubulavirus; Protein protein interaction; V protein

Indexed keywords

NUCLEOPROTEIN; UNCLASSIFIED DRUG; VIRUS PHOSPHOPROTEIN; VIRUS PROTEIN; VIRUS PROTEIN V;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; NONHUMAN; PARAMYXOVIRUS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SWINE;

ANIMALS; BINDING SITES; GENE EXPRESSION; GLUTATHIONE TRANSFERASE; NUCLEOCAPSID PROTEINS; NUCLEOPROTEINS; PHOSPHOPROTEINS; RECOMBINANT FUSION PROTEINS; RUBULAVIRUS; SWINE; VIRAL CORE PROTEINS; VIRAL PROTEINS;

PORCINE RUBULAVIRUS; RUBULAVIRUS; SUIDAE;

EID: 0037177036     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1702(01)00406-3     Document Type: Article

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3. Identification of the porcine paramyxovirus LPMV matrix protein gene: Comparative sequence analysis with other paramyxoviruses
4. The Sendai virus P gene expresses both an essential protein and an inhibitor of RNA synthesis by shuffling modules via mRNA editing
5. An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication
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14. The paramyxovirus, Sendai virus, V protein encodes a luxury function required for viral pathogenesis
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