scholarly journals Amino acid sequence and oligosaccharide distribution of the haemagglutinin from an early Hong Kong influenza virus variant A/Aichi/2/68 (X-31)

1981 ◽  
Vol 193 (3) ◽  
pp. 953-962 ◽  
Author(s):  
C W Ward ◽  
T A Dopheide
Keyword(s):  
Influenza Virus ◽  
Hong Kong ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Peptide Sequencing ◽  
Amino Acid Sequences ◽  
Hydrophobic Region ◽  
Virus Variant ◽  
The Individual ◽  
Polypeptide Chains

The amino acid sequence and oligosaccharide distribution for the haemagglutinin from the early Hong Kong influenza virus A/Aichi/2/68 (X-31) was investigated. The two polypeptide chains, HA1 and HA2, were fragmented by CNBr and enzymic digestion, and the amino acid sequence of each small peptide was deduced by comparing its chromatographic behaviour, electrophoretic mobility, amino acid composition and N-terminus with that of the corresponding peptide of the haemagglutinin of known structure from the influenza-virus variant A/Memphis/102/72. Those peptides in which changes were detected were sequenced fully. The complete amino acid sequence of the haemagglutinin HA1 chain (328 residues) and 188 of the 221 residues of the HA2 chain were established by this approach, and revealed only twelve differences between the amino acid sequences of variant-A/Aichi/68 and -A/Memphis/72 haemagglutinins. These occurred at positions 2, 3, 122, 144, 155, 158, 188, 207, 242 and 275 in the HA1 chain and 150 and 216 in the HA2 chain. The highly aggregated hydrophobic region (residues 180-121) near the C-terminal end of the HA2 chain was not resolved by peptide sequencing. The oligosaccharide distribution in variant-A/Aichi/68 haemagglutinin was identical with that found in that of A/Memphis/72, with sugar units attached at asparagine residues 8, 22 38, 81, 165 and 285 in the HA1 chain and 154 on the HA2 chain. The monosaccharide compositions of the individual carbohydrate units on variant-A/Aichi/68 haemagglutinin differed from those of the corresponding units in variant-A/Memphis/72 haemagglutinin, and evidence was found for heterogeneity in the oligosaccharide units attached at single glycosylation sites.

Amino acid sequence changes in the haemagglutinin of A/Hong Kong (H3N2) influenza virus during the period 1968–77

Nature ◽  
1980 ◽  
Vol 283 (5746) ◽  
pp. 454-457 ◽  
Author(s):  
W. G. Laver ◽  
G. M. Air ◽  
T. A. Dopheide ◽  
C. W. Ward
Keyword(s):  
Influenza Virus ◽  
Hong Kong ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
H3n2 Influenza ◽  
H3n2 Influenza Virus

scholarly journals An amino acid sequence in the active site of lipoamide dehydrogenase from pig heart

1974 ◽  
Vol 137 (3) ◽  
pp. 505-512 ◽  
Author(s):  
Joseph P. Brown ◽  
Richard N. Perham
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Amino Acid Sequences ◽  
Disulphide Bridge ◽  
Similar Sequence ◽  
Bacterial Enzyme ◽  
Oxoglutarate Dehydrogenase ◽  
Lipoamide Dehydrogenase ◽  
Polypeptide Chains

1. The two cysteine residues forming the disulphide bridge that comprises part of the active site of lipoamide dehydrogenase from pig heart were specifically labelled with iodo[2-14C]acetic acid. 2. A tryptic peptide containing these carboxymethylcysteine residues was isolated from digests of reduced and S-carboxymethylated lipoamide dehydrogenase and its amino acid sequence of 23 residues was determined. 3. The sequence is highly homologous with a similar sequence containing the active-site disulphide bridge of lipoamide dehydrogenase derived from the 2-oxoglutarate dehydrogenase complex of Escherichia coli (Crookes strain) and it is probable that, as in the bacterial enzyme, the disulphide bridge forms an intrachain loop containing six residues. The results indicate that the bacterial and mammalian proteins have a common genetic origin. 4. Amino acid sequences containing six other unique carboxymethylcysteine residues were also partly determined. 5. The analysis of the primary structure thus far is consistent with the view that the enzyme (mol.wt. approx. 110000) is composed of two identical polypeptide chains.

scholarly journals The Evolution of Vertebrate Fibrinogen

1977 ◽  
Author(s):  
Russell F. Doolittle
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Common Ancestor ◽  
Amino Acid Sequences ◽  
Polar Material ◽  
Prototype Structure ◽  
Polypeptide Chains ◽  
Fibrinogen Molecule ◽  
The Way

The fibrinogens of all vertebrates studied to date are comprised of three pairs of non-identical polypeptide chains.Moreover, in all of these cases--whether the molecule is isolated from a primitive fish or an advanced mammal--polymerization is induced by the thrombin-cata-lyzed removal of polar peptide material from the ami no-terminal segments of two of the three chains. Amino acid sequence studies on mammalian fibrinogen molecules have provided convincing support, however, for the notion that the three non-identical polypeptide chains have evolved from a common ancestor and also that the present chains have been elongated by a series of internal duplications.Thus, we are now in a position to speculate on the structure of the primordial fibrinogen molecule and how it could be gelled by a proteolytic event. The molecule must have been comprised of (two) bundles of three identical polypeptide chains, all of which must have been sensitive to the action of thrombin.Furthermore, symmetry arguments suggest that the way the three identical chains would have been bundled together is best approximated by a (disulfide-linked) three stranded rod. Given the multiple restraints on such a molecule, a reasonable scheme can be advanced for polymerization based on the removal of polar material from one end of the rod. The differences in amino acid sequences for the three chains comprising the present day fibrinogen molecules are such that the duplicative events leading to their divergence must have occurred more than 600 million years ago, or long before the origin of vertebrates. It will be of great interest if a primitive molecule can be found in some extant creature which approximates the prototype structure.

Versuche zur Bestimmung der serologisch determinanten Gruppen des Tabakmosaikvirus

1963 ◽  
Vol 18 (12) ◽  
pp. 1010-1014 ◽  
Author(s):  
F. A. Anderer
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Polypeptide Chain ◽  
Amino Acid Sequences ◽  
Virus Protein ◽  
Specific Antibodies ◽  
The Individual

Twenty peptides of tobacco mosaic virus protein covering the whole amino acid sequence of the polypeptide chain have been tested for their capacity to inhibit the quantitative precipitation of tobacco mosaic virus with the specific antibodies. Only four amino acid sequences, representing 15-20% of the polypeptide chain, have been found to diminish quantitative precipitation of TMV with anti TMV serum. Lack of additivity of the individual inhibition values gives evidence that the specific antibodies are not directed against isolated amino acid sequences.

scholarly journals Evolution of the Hong Kong influenza A sub-type. Structural relationships between the haemagglutinin from A/duck/Ukraine/1/63 (Hav 7) and the Hong Kong (H3) haemagglutinins

1981 ◽  
Vol 195 (1) ◽  
pp. 337-340 ◽  
Author(s):  
C W Ward ◽  
T A Dopheide
Keyword(s):  
Influenza Virus ◽  
Hong Kong ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Influenza A ◽  
Antigenic Drift ◽  
Amino Acid Sequence Analysis ◽  
Structural Relationships ◽  
The Relationship

The relationship between the haemagglutinin from the influenza virus A/duck/Ukraine/1/63 (Hav 7) and the human Hong Kong variants (H3) has been investigated. Amino-acid-sequence analysis shows that the Hav 7 haemagglutinin closely resembles the 1968 human H3 haemagglutinin in structure. However, the number of amino-acid-sequence differences (23) suggest that the Hong Kong haemagglutinin gene did not come directly from A/duck/Ukraine/1/63 but from a virus derived from it by antigenic drift during the period 1963-1968.

Amino-Acid Sequence of the αD- and ß-Polypeptide Chains of the Japanese Quail Hemoglobin

1993 ◽  
Vol 374 (1-6) ◽  
pp. 111-116 ◽  
Author(s):  
Yukinori EGUCHI ◽  
Yasutugu NAKASHIMA ◽  
Hiroshi TAKEI
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Japanese Quail ◽  
Polypeptide Chains

SOME ASPECTS OF THE STRUCTURE OF HEMOGLOBIN

1964 ◽  
Vol 42 (6) ◽  
pp. 755-762 ◽  
Author(s):  
David B. Smith
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Partial Amino Acid Sequence ◽  
Heme Pocket ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Kinetics Of ◽  
Β Chain

An outline of present ideas concerning the arrangement, folding, and chemistry of the polypeptide chains of hemoglobin is given with some references to present know ledge of myoglobin.New material includes a partial amino acid sequence of the β-chain of horse hemoglobin, details concerning the amino acids lining the heme pocket of horse hemoglobin, and the effects of carboxypeptidases A and B on horse oxy- and horse deoxy-hemoglobin. The kinetics of the latter reactions are not simple. The C-terminal amino acids are released more rapidly from the oxygenated form.

scholarly journals The amino acid sequence of cytochromes c-551 from three species of Pseudomonas

1973 ◽  
Vol 131 (3) ◽  
pp. 485-498 ◽  
Author(s):  
R. P. Ambler ◽  
Margaret Wynn
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Mitochondrial Cytochrome ◽  
Cytochromes C ◽  
Lending Library ◽  
Single Peptide

The amino acid sequences of the cytochromes c-551 from three species of Pseudomonas have been determined. Each resembles the protein from Pseudomonas strain P6009 (now known to be Pseudomonas aeruginosa, not Pseudomonas fluorescens) in containing 82 amino acids in a single peptide chain, with a haem group covalently attached to cysteine residues 12 and 15. In all four sequences 43 residues are identical. Although by bacteriological criteria the organisms are closely related, the differences between pairs of sequences range from 22% to 39%. These values should be compared with the differences in the sequence of mitochondrial cytochrome c between mammals and amphibians (about 18%) or between mammals and insects (about 33%). Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 50015 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 5.

scholarly journals Factor D̄ of the alternative pathway of human complement. Purification, alignment and N-terminal amino acid sequences of the major cyanogen bromide fragments, and localization of the serine residue at the active site

1980 ◽  
Vol 187 (3) ◽  
pp. 863-874 ◽  
Author(s):  
D M Johnson ◽  
J Gagnon ◽  
K B Reid
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Alternative Pathway ◽  
Amino Acid Sequences ◽  
Serine Residue ◽  
Amino Acid Sequence Analysis ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

The serine esterase factor D of the complement system was purified from outdated human plasma with a yield of 20% of the initial haemolytic activity found in serum. This represented an approx. 60 000-fold purification. The final product was homogeneous as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis (with an apparent mol.wt. of 24 000), its migration as a single component in a variety of fractionation procedures based on size and charge, and its N-terminal amino-acid-sequence analysis. The N-terminal amino acid sequence of the first 36 residues of the intact molecule was found to be homologous with the N-terminal amino acid sequences of the catalytic chains of other serine esterases. Factor D showed an especially strong homology (greater than 60% identity) with rat ‘group-specific protease’ [Woodbury, Katunuma, Kobayashi, Titani, & Neurath (1978) Biochemistry 17, 811-819] over the first 16 amino acid residues. This similarity is of interest since it is considered that both enzymes may be synthesized in their active, rather than zymogen, forms. The three major CNBr fragments of factor D, which had apparent mol.wts. of 15 800, 6600 and 1700, were purified and then aligned by N-terminal amino acid sequence analysis and amino acid analysis. By using factor D labelled with di-[1,3-14C]isopropylphosphofluoridate it was shown that the CNBr fragment of apparent mol.wt. 6600, which is located in the C-terminal region of factor D, contained the active serine residue. The amino acid sequence around this residue was determined.

scholarly journals Functional Analysis of PA Binding by Influenza A Virus PB1: Effects on Polymerase Activity and Viral Infectivity

2001 ◽  
Vol 75 (17) ◽  
pp. 8127-8136 ◽  
Author(s):  
Daniel R. Perez ◽  
Ruben O. Donis
Keyword(s):  
Amino Acids ◽  
Influenza Virus ◽  
Amino Acid ◽  
Viral Replication ◽  
Influenza A Virus ◽  
Influenza A ◽  
Amino Acid Sequences ◽  
Influenza Viruses ◽  
Virus Growth ◽  
Transcription And Replication

ABSTRACT Influenza A virus expresses three viral polymerase (P) subunits—PB1, PB2, and PA—all of which are essential for RNA and viral replication. The functions of P proteins in transcription and replication have been partially elucidated, yet some of these functions seem to be dependent on the formation of a heterotrimer for optimal viral RNA transcription and replication. Although it is conceivable that heterotrimer subunit interactions may allow a more efficient catalysis, direct evidence of their essentiality for viral replication is lacking. Biochemical studies addressing the molecular anatomy of the P complexes have revealed direct interactions between PB1 and PB2 as well as between PB1 and PA. Previous studies have shown that the N-terminal 48 amino acids of PB1, termed domain α, contain the residues required for binding PA. We report here the refined mapping of the amino acid sequences within this small region of PB1 that are indispensable for binding PA by deletion mutagenesis of PB1 in a two-hybrid assay. Subsequently, we used site-directed mutagenesis to identify the critical amino acid residues of PB1 for interaction with PA in vivo. The first 12 amino acids of PB1 were found to constitute the core of the interaction interface, thus narrowing the previous boundaries of domain α. The role of the minimal PB1 domain α in influenza virus gene expression and genome replication was subsequently analyzed by evaluating the activity of a set of PB1 mutants in a model reporter minigenome system. A strong correlation was observed between a functional PA binding site on PB1 and P activity. Influenza viruses bearing mutant PB1 genes were recovered using a plasmid-based influenza virus reverse genetics system. Interestingly, mutations that rendered PB1 unable to bind PA were either nonviable or severely growth impaired. These data are consistent with an essential role for the N terminus of PB1 in binding PA, P activity, and virus growth.

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