Posttranslational processing and identification of a neutralization domain of the GP4 protein encoded by ORF4 of Lelystad virus

GP4 is a minor structural glycoprotein encoded by ORF4 of Lelystad virus (LV). When it was immunoprecipitated from cell lysates and extracellular virus of CL2621 cells infected with LV it was shown to have an apparent molecular mass of approximately 28 and 31 kDa, respectively. This difference in si...

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Bibliographic Details
Published in:Journal of Virology 1997-08, Vol.71 (8), p.6061-6067
Main Authors: Meulenberg, J J, van Nieuwstadt, A P, van Essen-Zandbergen, A, Langeveld, J P
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antibodies, Monoclonal - immunology
antigene
antigenos
antigens
ID Lelystad, Institute for Animal Science and Health
ID-Lelystad, Instituut voor Dierhouderij en Diergezondheid
lelystad virus
Molecular Sequence Data
Neutralization Tests
Open Reading Frames
Porcine respiratory and reproductive syndrome virus - genetics
Protein Processing, Post-Translational
Rabbits
Swine
Viral Structural Proteins - biosynthesis
Viral Structural Proteins - chemistry
Viral Structural Proteins - immunology
virus de lelystad
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Description
Summary:GP4 is a minor structural glycoprotein encoded by ORF4 of Lelystad virus (LV). When it was immunoprecipitated from cell lysates and extracellular virus of CL2621 cells infected with LV it was shown to have an apparent molecular mass of approximately 28 and 31 kDa, respectively. This difference in size occurred because its core N-glycans were modified to complex type N-glycans during the transport of the protein through the endoplasmic reticulum and Golgi compartment. A panel of 15 neutralizing monoclonal antibodies (MAbs) reacted with the native GP4 protein expressed by LV and the recombinant GP4 protein expressed in a Semliki Forest virus expression system. However these MAbs did not react with the GP4 protein of U.S. isolate VR2332. To map the binding site of the MAbs chimeric constructs composed of ORF4 of LV and VR2332 were generated. The reactivity of these constructs indicated that all the MAbs were directed against a region spanning amino acids 40 to 79 of the GP4 protein of LV. Six MAbs reacted with solid-phase synthetic dodecapeptides. The core of this site consists of amino acids 59 to 67 (SAAQEKISF). Comparison of the amino acid sequences of GP4 proteins from various European and North American isolates indicated that the neutralization domain spanning amino acids 40 to 79 is the most variable region of GP4. The neutralization domain of GP4, described here, is the first identified for LV.
ISSN:0022-538X
1098-5514
DOI:10.1128/jvi.71.8.6061-6067.1997