Virus Research, 8 (1987) 205-215 Elsevier 205 VRR 00355 Molecular cloning and sequence analysis of the human parainfluenza 3 virus genes encoding the surface glycoproteins, F and HN Mark S. Galinski, Michael A. Mink and Marcel W. Pons Division of Molecular Virology, James N. Gamble Institute of Medical Research, Cincinnati, Ohio, U.S.A. (Accepted for publication 22 May 1987) The sequence of the genes encoding the fusion (F) and hemagglutinin-neur- aminidase (HN) glycoproteins of the human parainfluenza 3 virus was determined by molecular cloning. The genes were cloned by primer extension using genomic 50 S RNA as the template. A series of four overlapping clones was generated from the 3’ end of the fusion gene which extended across the gene end and intergenic boundaries of the F-HN and HN-L genes. The F gene extends 1851 nucleotides (inclusive of the putative transcription initiation and polyadenylation signals) and encodes a protein consisting of 539 amino acids (mol wt 60067). This protein contains four potential sites for N-linked glycosylation in the Ft subunit polypeptide and none in the F, subunit polypeptide. The lack of a potential site of glycosylation in F2 makes this protein unique compared to other reported paramyxoviral F proteins. The HN gene extends 1888 nucleotides and encodes a protein consisting of 572 ammo acids (mol wt 64255). This protein contains four potential sites for N-linked glycosylation. Paminfluenza 3 virus; Hemagglutinin-neuraminidase gene sequence; Fusion gene sequence; Glycoprotein gene sequences zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONM Introduction Recently, the molecular cloning and sequence analysis of the human parainfluenza 3 virus (PF3) has provided the gene sequences for all but one of the structural Correspondence to: M. Gabski, Divn. of Molecular Virology, James N. Gamble Institute of Medical Research, 2141 Auburn Ave., Cincinnati, OH 45219, U.S.A. 0168-1702/87/$03.50 6 1987 Elsevier Science Publishers B.V. (Biomedical Division)