Immunological Characterization of the Feline Herpesvirus-1 Glycoprotein B and Analysis of Its Deduced Amino Acid Sequence

A lectin was isolated from the pod saline extract of Caesalpinia tinctoria by dialoconcentration on Centripep-10 and affinity chromatography on chitin column. The purified lectin was partially characterized with respect to its biochemical and structural properties. It contains 8.3 % of carbohydrate and exhibited an agglutinating activity against human erythrocytes (ABO groups). Its amino acid composition was characterized by a great number of acidic and hydrophobic residues and the estimated molecular mass was 12.5 kDa. The presence of only one N-terminal amino acid sequence (D¹-V-P-A-Y-V-Y-V-H-F10-G-F-G-E-E-H-R -D-V-F20-D), showed the homogeneity of the purified lectin. The far-ultraviolet circular dichroism (CD) spectrum of lectin indicated that it contains 10 % a-helix, 38 % b-sheet, 28 % unordered form and 6 % of P II (poly-L-proline II helix conformation).

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Characterization of a major early gene from the human cytomegalovirus long inverted repeat; predicted amino acid sequence of a 30-kDa protein encoded by the 1.2-kb mRNA

Virology ◽

10.1016/0042-6822(86)90177-7 ◽

1986 ◽

Vol 155 (1) ◽

pp. 172-182 ◽

Cited By ~ 9

Author(s):

Nancy I. Hutchinson ◽

Michael J. Tocci

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Human Cytomegalovirus ◽

Inverted Repeat ◽

Early Gene ◽

Predicted Amino Acid Sequence

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Characterization of N-terminal amino acid sequence of monoclonal nonspecific suppressor factor

Cellular Immunology ◽

10.1016/0008-8749(92)90107-z ◽

1992 ◽

Vol 139 (1) ◽

pp. 139-144 ◽

Cited By ~ 6

Author(s):

Morihiko Nakamura ◽

Hiroyuki Ogawa ◽

Tokugoro Tsunematsu

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Terminal Amino Acid ◽

Suppressor Factor ◽

Terminal Amino ◽

Terminal Amino Acid Sequence

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Characterization of two newly isolated Staphylococcus aureus bacteriophages from Japan belonging to the genus Silviavirus

Archives of Virology ◽

10.1007/s00705-020-04749-6 ◽

2020 ◽

Vol 165 (10) ◽

pp. 2355-2359

Author(s):

Naoya Kitamura ◽

Eri Sasabe ◽

Shigenobu Matsuzaki ◽

Masanori Daibata ◽

Tetsuya Yamamoto

Keyword(s):

Staphylococcus Aureus ◽

Amino Acid ◽

Amino Acid Sequence ◽

Dna Sequences ◽

Related Gene ◽

Bacteriophage Therapy ◽

Dna Rearrangements ◽

Site Specific

Abstract Two Staphylococcus aureus bacteriophages, KSAP7 and KSAP11, were isolated from sewage and characterized. Based on morphology and DNA sequences, they were assigned to the genus Silviavirus, subfamily Twortvirinae, family Herelleviridae, whose members are hypothesized to be suitable for bacteriophage therapy. The KSAP7 and KSAP11 genomes were 137,950 and 138,307 bp in size, respectively. Although their DNA sequences were almost identical, evidence of site-specific DNA rearrangements was found in two regions. Changes in the number of PIEPEK amino acid sequence repeats encoded by orf10 and the insertion/deletion of a 541-bp sequence that includes a possible tail-related gene were identified.

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Biochemical characterization of a second family of human Ia molecules, HLA-DS, equivalent to murine I-A subregion molecules.

Journal of Experimental Medicine ◽

10.1084/jem.156.2.550 ◽

1982 ◽

Vol 156 (2) ◽

pp. 550-566 ◽

Cited By ~ 145

Author(s):

S M Goyert ◽

J E Shively ◽

J Silver

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Amino Acid Sequence Identity ◽

Biochemical Characterization ◽

Amino Acid Sequence Homology ◽

Molecular Weights ◽

Hla Dr ◽

D Region ◽

Polypeptide Chains

In mice, two families of structurally distinct Ia molecules, one designated I-A and the other I-E, have been identified and characterized. The HLA-DR molecules represent one family of human Ia molecules equivalent to the murine I-E molecules on the basis of amino acid sequence homology. We describe the isolation and biochemical characterization of a second family of human Ia molecules, designated HLA-DS for second D-region locus, equivalent to the murine I-A molecules. The human HLA-DS molecules consist of two polypeptide chains, DS alpha (37,000 mol wt) and DS beta (29,000 mol wt), with 73% amino acid sequence identity to the murine I-A molecules. Furthermore, the HLA-DS molecules are closely linked genetically to HLA-DR molecules, a situation analogous to that observed in mice. The similarity in molecular weights of the DR and DS molecules might explain why others have failed to identify the latter in man.

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