Human parainfluenza type 3 virus hemagglutinin-neuraminidase glycoprotein: nucleotide sequence of mRNA and limited amino acid sequence of the purified protein

Abstract

The nucleotide sequence of mRNA for the hemagglutinin-neuraminidase (HN) protein of human parainfluenza type 3 virus obtained from the corresponding cDNA clone had a single long open reading frame encoding a putative protein of 64,254 daltons consisting of 572 amino acids. The deduced protein sequence was confirmed by limited N-terminal amino acid microsequencing of CNBr cleavage fragments of native HN that was purified by immunoprecipitation. The HN protein is moderately hydrophobic and has four potential sites (Asn-X-Ser/Thr) of N-glycosylation in the C-terminal half of the molecule. It is devoid of both the N-terminal signal sequence and the C-terminal membrane anchorage domain characteristic of the hemagglutinin of influenza virus and the fusion (F0) protein of the paramyxoviruses. Instead, it has a single prominent hydrophobic region capable of membrane insertion beginning at 32 residues from the N terminus. This N-terminal membrane insertion is similar to that of influenza virus neuraminidase and the recently reported structures of HN proteins of Sendai virus and simian virus 5.

A molecular epidemiological study of human parainfluenza virus type 3 at a tertiary university hospital during 2013–2015 in Catalonia, Spain

“…Phylogenetic group C remained as the most dynamic and widespread group worldwide (Almajhdi, 2015;Mao et al, 2012). Nucleotide sequences analyzed in comparison with different international strains demonstrated an association with some Chinese strains (C3a) (Mao et al, 2012) and Saudi Arabia strains (C1b and C5) (Almajhdi, 2015;Almajhdi et al, 2012), whereas no association with strains from America (Elango et al, 1986;van Wyke Coelingh et al, 1988), India (unpublished) or Australia (Lawrence et al, 2004;van Wyke Coelingh et al, 1988) was observed. In addition, a new lineage (C1c) was first described in the present study.…”

Chimeric human parainfluenza virus bearing the Ebola virus glycoprotein as the sole surface protein is immunogenic and highly protective against Ebola virus challenge

“…Thus, infectivity of this chimeric virus would depend on incorporation of EBOV GP, which directs both attachment and fusion, into the particle. EBOV GP is a type I transmembrane protein that has an unusually short C-terminal cytoplasmic tail (CT) KFVF (Sanchez et al, 1993) that bears no sequence similarity to the much longer 23 amino acid C-terminal CT of the type I HPIV3 F protein (Spriggs et al, 1986), or the 31 amino acid N-terminal CT of the type II HPIV3 HN protein (Elango et al, 1986). The efficiency of incorporation of a foreign glycoprotein into a virus particle can be influenced by its CT, such that replacement of the foreign CT with that from an endogenous glycoprotein can increase incorporation (Tao et al, 2000).…”

Lentiviruses inefficiently incorporate human parainfluenza type 3 envelope proteins

“…Steric hindrance between the cytoplasmic tail of these proteins and the capsids of the budding virus particles is one likely mechanism by which proteins are actively excluded from lentiviruses (Henriksson et al, 1999). Although we can not rule out the possibility that HPIV3 Env are actively excluded from lentiviruses, it seems unlikely that steric hindrance plays a role since both HPIV3-HN and -F have short cytoplasmic domains (31 and 23 amino acids, respectively (Elango et al, 1986;Spriggs et al, 1986)), and envelope proteins with naturally short cytoplasmic tails such as MuLV Env, and envelope proteins from HIV-2 and SIV with long cytoplasmic tails that have been truncated, have been shown to be efficiently incorporated into lentiviral particles (Freed and Martin, 1995;Zingler and Littman, 1993).…”