Complete nucleotide sequence of an influenza virus haemagglutinin gene from cloned DNA

Porter, Alan G.; Barber, C. E.; Carey, N. H.; Hallewell, Robert A.; Threlfall, G.; Emtage, J.S.

doi:10.1038/282471a0

Cited by 287 publications

(126 citation statements)

References 48 publications

Supporting

Mentioning

120

Contrasting

Order By: Relevance

“…The presence of the sequence 5'-AGCAAAAGCAGG at the 5' end of the pVHA14 insert proves that the complete information starting from the 3' end of the viral RNA (negative strand) has been cloned, as the complementary sequence has been found at the 3' end of all influenza A viral RNAs studied thus far (Skehel and Hay, 1978;Robertson, 1979;Both and Air, 1979;Desselberger et al, 1980;McCauley et al, 1979;Porter et al, 1979). The only nucleotide which is variable in the first segment of 12 residues is nucleotide 4, which can be A (FPV; X31; HA, NP and NS from PR8; HA from A/RI/5/57) or G (the five other genes of PR8).…”

Section: General Features Of the Nucleotide Sequencementioning

confidence: 85%

“…The first 22 nucleotides at the 5' end of the virion RNA--except for residues 14, 15 and 16--are highly conserved in all genes of all A-type viruses examined thus far (Skehel and Hay, 1978;Robertson, 1979;Desselberger et al, 1980). The addition of 23 residues makes the exact length of the viral RNA 1.768 nucleotides, which is very similar to the length of the FPV hemagglutinin RNA--that is, 1742 nucleotides (Porter et al, 1979 …”

Section: General Features Of the Nucleotide Sequencementioning

confidence: 91%

“…Now we have applied this technique to the negative-stranded (and nonpolyadenylated) viral RNA corresponding to the hemagglutinin gene of a recent human influenza H3N2 strain, A/Victoria/3/75. The complete sequence is compared with the sequence of an animal strain (Fowl Plague Virus) determined by a similar procedure (Porter et al, 1979) and with the available amino acid sequence data of two human strains mentioned above: an H3N2 strain and an H2N2 strain .…”

Section: Introductionmentioning

confidence: 99%

“…The results are compared with partial amino acid sequences from another H3 strain, A / M e m p h i s / 1 0 2 / 7 2 and from an H2 strain McCauley et al, 1979;Waterfield et al, 1979;M. Waterfield, personal communication) and with the complete amino acid sequence deduced from another cloned influenza A hemagglutinin gene, that of Fowl Plague Virus (Porter et al, 1979). Homologous sequences are boxed and dotted lines indicate potential sites for carbohydrate attachment at asparagine residues in Asn-X-Ser or Asn-X-Thr sequences.…”

mentioning

confidence: 99%

“…The majority of picornaviruses (Porter et al, 1978) and one of the VSV mRNAs (McGeoch and Turnbull, 1978) also do not have this signal. Porter et al (1979) have noted that the 3' terminal segment of the cloned insert contains several mutations compared to the bona fide virion RNA. This result can be explained on the basis of the terminal hairpin used for the self-primed synthesis of the second DNA strand, followed by a correction of base mismatches in the bacterial cell.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Complete structure of the hemagglutinin gene from the human influenza A/Victoria/3/75 (H3N2) strain as determined from cloned DNA

Jou

Verhoeyen

Devos

et al. 1980

Cell

219

View full text Add to dashboard Cite

SummaryThe complete sequence of a hemagglutinin (HA) gene of a recent human influenza A strain, A/Victoria/3/75, is 1768 nucleotides long and contains the information for 567 amino acids. It codes for a signal peptide of 16 amino acids, the HA1 chain of the mature hemagglutinin of 329 amino acids, a connecting region between HA1 and HA2 consisting of a single arginine residue and the HA2 portion of 221 amino acids. The sequence is compared with the hemagglutinin of two members of other subtypes, the human H2 strain A/Jap/305/57 and the avian Havl strain A/FPV/Rostock/34, and with one of the same H3 subtype, A/Memphis/3/72. To align the HA1 chain of different major subtypes several deletions/insertions of single amino acids must be invoked, but two more extensive differences are found at both ends, one leading to an extension of the amino terminal sequence of HA1 and the other (four residues) occurring in the region processed away between HA1 and HA2. Comparison of the HA1 of two H3 strains suggests that drift probably depends on single base mutations, some of which change antigenic determinants. The HA2 region, which apparently is not involved in the immune response, is highly conserved even between different subtypes, and single base substitutions account for all the observed diversity. A hydrophobic segment of 24 residues is present in the same position close to the carboxyl terminus of HA2 in both Victoria and FPV, and presumably functions in implantation into the lipid bilayer. The many conserved features not only in HA2 but also in HA1 suggest a rather rigid architecture for the whole hemagglutinin molecule.

show abstract

Section: General Features Of the Nucleotide Sequencementioning

confidence: 85%

Section: General Features Of the Nucleotide Sequencementioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Complete structure of the hemagglutinin gene from the human influenza A/Victoria/3/75 (H3N2) strain as determined from cloned DNA

Jou

Verhoeyen

Devos

et al. 1980

Cell

219

View full text Add to dashboard Cite

show abstract

Mean‐square helical hydrophobic moments in partially ordered proteins

Hamed

Mattice

1984

Biopolymers

View full text Add to dashboard Cite

Synopsis Helical hydrophobic moment ratios, ( h 2 ) / ( H 2 ) ,have been evaluated for 34 polypeptides under conditions where the helix content is dictated solely by the short-range interactions operative in aqueous media. The mean-square helical hydrophobic moment is denoted by ( h 2 ) , and ( H 2 ) is the averaged of the squared hydrophobicities. This ratio would he one in absence of any correlation in the hydrophobicities of amino acid residues in helices. The ( h 2 ) / ( H 2 ) tend to be substantially larger than values of the analogous ratio formulated for the mean-square dipole moments of typical synthetic polymers. For 24 of the 34 polypeptide chains considered, ( h 2 ) / ( H 2 ) is found to be greater than one, indicating a tendency to form helices with amphiphilic character. The ratio is exceptionally large in the case of the &he-molysins. It is also large for two other surface-active peptides, for two of the four apolipoproteins examined, and for myohemerythrin.is found for melittins. If melittins is to form helices with large ( h 2 ) / ( H 2 ) , the configurational statistics must be governed by effects in addition to those short-range interactions that occur when water is the solvent. INTRODUCTIONHydrophobic interactions contribute to stabilization of ordered structures formed by proteins in biological systems. One quantitative assessment of the strength of hydrophobic interactions is in terms of hydrophobicities assigned to individual amino acid residues.lX2 Several such assignments have been p r o p~s e d .~-~ The set of hydrophobicities presented in Table I is based on partitioning of amino acid residues between the interior and surface in proteins of known conformation.The nature of the surfaces of an a-helical segment can be described in terms of hydrophobicities of the consistent amino acid residues. The simplest description is provided by the two-dimensional helical wheel, in which the array of amino acid residue side chains is viewed down the principal axis of the helix.8 When viewed in this manner, certain helical segments in myoglobin and hemoglobing are found to have one surface that is predominantly hydrophilic and an opposing surface that is predominantly hydrophobic. A helix of this type would be expected to be a strong candidate for a site at the surface of a globular protein.A quantitative analysis of information contained in the two-dimensional helical wheel has been presented by Eisenberg et al.7,10 A more elaborate computational scheme is required to analyze the potential amphiphilic character of helices when a unique conformation cannot be specified for the macromolecule. This situation arises if a multitude of conformations make significant contributions to the configuration partition function. I t also occurs when a single (but unknown) conformation dominates the configuration partition function. In these cases, each chain configuration should provide an appropriately weighed contribution to the quantity evaluated. Evaluation of a suitable measure of the average amphiphilic c...

show abstract

Evidence for similar function of transmembrane segments in receptor and membrane‐anchored proteins

Deber

Hsu.

et al. 1988

Biopolymers

View full text Add to dashboard Cite

SynopsisTransmembrane (TM) regions of receptor proteins should have unique structural and/or chemical characteristics if these regions contain residues functional in TM signal transduction.However, in a survey of the membrane-occurring residues in 37 integral membrane proteins, we found that amino acid compositions of TM regions of receptor proteins ( n = 11) could not be distinguished statistically from corresponding regions of membrane-anchored proteins (e.g., recognition molecules) with a functional external domain attached to a single hydrophobic membranespanning anchor segment ( n = 16). TM regions in both categories of proteins differed from the compositions of TM regions in membrane-transport proteins ( n = 10). The analysis implies that TM regions in receptor proteins may function mainly to anchor (and position) receptors in their cellular membranes, and therefore residues in receptors that participate in signal transduction need not be restricted to these regions. In addition to mechanisms involving receptor aggregation, ligand-activated conformational perturbation of a receptor external aqueous domain, resulting in membrane penetration of hydrophobic segment@) of this domain to produce intramembranous contact with its cytoplasmic domain, is hypothesized as a further possible mode of signal transduction.

show abstract

Complete nucleotide sequence of an influenza virus haemagglutinin gene from cloned DNA

Cited by 287 publications

References 48 publications

Complete structure of the hemagglutinin gene from the human influenza A/Victoria/3/75 (H3N2) strain as determined from cloned DNA

Complete structure of the hemagglutinin gene from the human influenza A/Victoria/3/75 (H3N2) strain as determined from cloned DNA

Mean‐square helical hydrophobic moments in partially ordered proteins

Evidence for similar function of transmembrane segments in receptor and membrane‐anchored proteins

Contact Info

Product

Resources

About