The polypeptides of influenza virus

Lazdins, Ieva; Haslam, Elizabeth A.; White, David O.

doi:10.1016/0042-6822(72)90532-6

Cited by 45 publications

(6 citation statements)

References 15 publications

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“…are interconnected by disulfide bonds and appear as an HA band in the absence of sulfhydryl compounds. An oligomeric form(s) of influenza neuraminidase which could be dissociated by sulfhydryl compounds has also been reported (19)(20)(21).…”

Section: Mode Of Binding Of Interpeptide Disulfide Bond-linked Fragmementioning

confidence: 92%

The Presence and Cleavage of Interpeptide Disulfide: Bonds in Viral Glycoproteins1

Ozawa¹,

Asano²,

Okada

1979

The Journal of Biochemistry

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The presence and nature of interpeptide disulfide bonds in HANA (Aemagglutinin and neuraminidase) glycoprotein and F (/usion) glycoprotein of HVJ (Sendai virus) are described. In the case of HANA, subunits of the same or very similar molecular weight were interconnected with a disulfide bond(s). Cleavage of the bond(s) can easily be achieved by the addition of 1 min dithiothreitol with concomitant loss of the biological activities of the glycoprotein. After splitting of the interconnecting bonds, all the HANA protein subunits remained bound on the viral membrane. To observe the cleavage of the interpeptide disulfide bond between the F x and F 2 subunits of F glycoprotein, higher concentrations of sulfhydryl compounds were required than were necessary for HANA protein. Splitting of the disulfide bond under either denaturing or nondenaturing conditions failed to release both segments of F protein from the virion. Therefore, F glycoprotein seems to have at least two membrane binding sites, one on F 1 and the other on F 2. On the other hand, the disulfide bond which connects the HAi and HA 2 subunits of influenza virus is hardly cleaved under non-denaturing conditions. Addition of 8 M urea or 6 M guanidine HC1, which completely inactivates HA activity, was necessary for the splitting of this disulfide bond by thiol compounds. Interestingly, the HA t subunit was released from the virion after the cleavage. Thus, unlike F t and F 2 of HVJ, the HA t subunit seems to have no hydrophobic binding site to the membrane. A mode! for the arrangement of these subunits on the viral membrane is proposed. Viral membranes have been used as a unique ability to induce cell fusion (i), HVJ (Sendai model system for the study of membrane structure virus) is a particularly interesting object for such and membrane assembly {1, 2). Because of its studies.

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Section: Mode Of Binding Of Interpeptide Disulfide Bond-linked Fragmementioning

confidence: 92%

The Presence and Cleavage of Interpeptide Disulfide: Bonds in Viral Glycoproteins1

Ozawa¹,

Asano²,

Okada

1979

The Journal of Biochemistry

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“…The knob structure can no longer aggregate with itself or with HA molecules, indicating that the hydrophobic regions of the molecule have been removed by proteolysis. The MW of the portion of the NA monomer which remains associated with the envelope after trypsin treatment was estimated to be 7000 daltons by Lazdins et al (1972) and 12,000 daltons by Wrigley et al (1973). Presumably, this portion functions to attach the NA molecule to the virion and plays no role in the enzymic properties.…”

Section: Influenza Virus Glycoproteinsmentioning

confidence: 99%

“…The oblong head is approximately 5 x 8.5 nm, and it is attached to a fiber approximately 10 nm long. The NA spike has a MW of approximately 240,000 daltons and is comprised of four NA polypeptides each having a MW of approximately 58,000 daltons; two NA polypeptides appear to be linked by disulfide bonds to form dimers, which are thought in turn to aggregate by noncovalent bonds to form the tetrameric spike (Bucher and Kilbourne, 1972;Lazdins et al, 1972). The amino acid composition of the NA has been determined, and it has a cysteine content significantly higher than that of the other viral polypeptides (Laver and Baker, 1972).…”

Section: Influenza Virus Glycoproteinsmentioning

confidence: 99%

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Membrane Glycoproteins of Enveloped Viruses

Compans

Kemp

1978

Current Topics in Membranes and Transport

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“…It projects from the surface of virions as a tetramer of identical molecules with a monomer molecular weight of58,000-68,000, depending on the virus (10)(11)(12)(13). Protease treatment releases the tetrameric head from the membrane-associated portion of the spike; this head has enzymatic and antigenic activities and a monomer molecular weight of 48,000-58,000 (10,12).…”

mentioning

confidence: 99%

Complete nucleotide sequence of the neuraminidase gene of influenza B virus.

Shaw

Lamb

Erickson

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

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The complete nucleotide sequence of the neuraminidase gene of influenza virus B/Lee/40 was derived from a cloned cDNA copy of virion RNA segment 6 and its corresponding mRNA. The RNA segment contains 1,557 virus-specific nucleotides, and the protein encoded by the longest open reading frame has a total of 466 amino acids with a molecular weight of 51,721. As is the case with the influenza A virus neuraminidases, the deduced amino acid sequence of the influenza B protein includes a single hydrophobic region near the amino terminus which would be capable of spanning the lipid bilayer of the viral or cell membrane. There are four potential glycosylation sites in the protein, two of which are near the amino-terminal hydrophobic region. Comparisons of the nucleotide and amino acid sequences with those of influenza A virus neuraminidases revealed seven regions of extensive homology within the central portion of the molecules, including 12 conserved cysteine residues. Five other cysteine residues in the terminal portions were also conserved.

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The polypeptides of influenza virus

Cited by 45 publications

References 15 publications

The Presence and Cleavage of Interpeptide Disulfide: Bonds in Viral Glycoproteins1

The Presence and Cleavage of Interpeptide Disulfide: Bonds in Viral Glycoproteins1

Membrane Glycoproteins of Enveloped Viruses

Complete nucleotide sequence of the neuraminidase gene of influenza B virus.

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