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At least 19 recordsLinked to original sources
PubMed1979

Antigenic determinants of influenza virus hemagglutinin. II. Antigenic reactivity of the isolated N-terminal cyanogen bromide peptide of A/Memphis/72 hemagglutinin heavy chain.

Gel filtration of a cyanogen bromide digest of pure intact hemagglutinin from A/Memphis/102/72 influenza virus allowed the isolation of a variety of fragments. One of these fragments consists of three cyanogen bromide peptides (CNl and CN3 from HA1, and CNl from HA2) which remain linked together by disulphide bonds. This fragment was found to be antigenically active, as it was able to form antigen-antibody complexes (detected by affinity chromatography of radioiodinated peptide-IgG mixtures on protein A-Sepharose) with IgG directed against the protein moiety of viral hemagglutinin. The three cyanogen bromide peptides present in this disulphide-linked fragment were separated by gel filtration, carried out under reducing conditions, and tested for antigenic activity after controlled reoxidation of the individual peptides. Only one cyanogen bromide peptide, CNl from HA1, showed significant binding to antibody. The results indicate that antigenic activity of A/Mem/1O2/72 hemagglutinin resides within the N-terminal 170 amino acid residues of the hemagglutinin heavy chain.

Antibodies, Viral↗
PubMedDate not supplied

[Study of the antigenic specificity of hemagglutinin of influenza viruses type A by quantitative radioimmunoassay. Comparative study of differences in the specificity of H3 hemagglutinin in epidemiologically active strains].

Comparative radioimmunoassays (RIA) of hemagglutinin of influenza type A viruses were carried out. The RIA was shown to detect definite type differences of influenza A and B virus hemagglutinin and subtype differences (HO and H3), as well as to determine both qualitative and quantitative characteristics of renewal of determinants within the antigenic drift. The A/Victoria/3/75 strain was found to have more renewed determinants than the A/Scotland/870/74 strain but less than the A/Victoria/112/76 strain which could be considered as a next drift variant. The epidemic strains circulating after 1972 had no more than 10% of the antigenic determinants characteristics of the original A/Hong Kong/1/68 strain. One of the advantages of the RIA was demonstrated to be its high sensitivity and economy as the specific antiserum can be used in dilutions 1:20,000 and higher. The test antigens may be both freshly isolated strains and virus-containing fluids showing no hemagglutinating activity (a titer in HA test 1:0).

Antigens, Viral↗
PubMed1976

Separation and characterization of two distinct hemagglutinins contained in purified leukocytosis-promoting factor from Bordetella pertussis.

1. The leukocytosis-promoting factor of Bordetella pertussis was found to contain two hemagglutinins with different susceptibilities to papain and separable from each other by agarose gel filtration with Tris - HCl buffer containing 1 M NaCl. 2. One hemagglutinin, referred to as hemagglutinin HA, had a high hemagglutinating activity, but neither leukocytosis-promoting nor histamine-sensitizing activity. The other hemagglutinin, referred to as hemagglutinin LPF appeared to be identical with the leukocytosis-promoting factor and possessed a low hemagglutinating and high leukocytosis-promoting and histamine-sensitizing activities. 3. The hemagglutinating activity of hemagglutinin HA was highly sensitive to papain. The hemagglutinating, leukocytosis-promoting, and histamine-sensitizing activities of hemagglutinin LPF were fairly resistant to the enzyme. 4. The two hemagglutinins were distinct from each other in immunological and chemical properties. 5. Morphologically, hemagglutinin HA showed itself to be filamentous molecules of approx. 2 X 40 nm, while hemagglutinin LPF comprised of spherical molecules of approx. 6 nm diameter. 6. The molecular weight values of hemagglutinin HA estimated by sodium dodecylsulfate polyacrylamide gel electrophoresis and sucrose density gradient centrifugation were approx. 126 000 and 133 000, respectively. Those of hemagglutinin LPF estimated by polyacrylamide gel electrophoreis at pH 4.5, sucrose density gradient centrifugation and gel filtration on a 10% agarose column were 107 000, 103 000 and 30 000, respectively. A possible reason for obtaining such a low molecular weight value by gel filtration is discussed.

Agglutinins↗
PubMed1979

Specificity of cytotoxicity T cells directed to influenza virus hemagglutinin.

Purified type A influenza viral hemagglutinin stimulates an in vitro cell-mediated cytotoxic cell response that exhibits a high degree of specificity for the immunizing hemagglutinin. The response magnitude is proportional to the hemagglutinin dose used for stimulation. The lytic activity of the effector cells is H-2 restricted. Analysis of the specificity of the response indicated that these cytotoxic T cells readily distinguish target cells expressing serologically unrelated hemagglutinin from target cells bearing hemagglutinins serologically related to the stimulating hemagglutinin. Further analysis of the fine specificity of cytotoxic T-cell recognition with serologically cross-reactive type A influenza hemagglutinins revealed a hierarchy of cross-reactivity among these hemagglutinins that was the converse of the serologic hierarchy. These results are discussed in terms of possible differences and similarities in the specificity repertoire of cytotoxic T cells and antibodies. Possible implications of these findings from the standpoint of cytotoxic T-cell induction are also discussed.

Animals↗
PubMed1977

Mannose-binding hemagglutinins in extracts of Pseudomonas aeruginosa.

Mannose-binding hemagglutinins were found in the extracts of a pyocyanin-forming Pseudomonas aeruginosa, which contain galactose-specific hemagglutinins. They were purified simultaneously with the latter proteins by heating to 70 degrees C, precipitating with ammonium sulfate, application to a Sepharose 4B column, and elution from it by 0.05 M mannose. The mannose-specific hemagglutinins were shown to be similar to the galactophilic ones in (a) being glycoproteins of very low molecular weight (about 11 000 by SDS gel electrophoresis), (b) their tendency to aggregate, and (c) their ability to effect stronger agglutination of erythrocytes treated with papain than of untreated ones. They were found to resemble them also in their reaction with simple sugars and interactions with divalent cations, which are essential for their activity. In these properties, as well as in their relative resistance to heat and to proteolytic enzymes, these two types of bacterial hemagglutinins are like most of the plant, contrasted with the animal, hemagglutinins. The reactions with mannose and mannose-bearing compounds (yeast mannan, horseradish peroxidase (EC 1.11.1.7), and serum globulins), which are not shared with the galactophilic Pseudomonas hemagglutinins, indicate a relationship of the mannose-binding protein of Pseudomonas to the plant lectin concanavalin A. The mannose-binding hemagglutinins do not exhibit identical cell-agglutinating spectra owing to difference in profiles of sugar specificity and relative affinity to mannose derivatives compared with free mannose.

Agglutinins↗
PubMed1975

Purification and properties of an anti-B hemagglutinin produced by Streptomyces sp.

An anti-B hemagglutinin was purified to homogeneity from the culture filtrate of a strain of Streptomyces sp. by affinity chromatography. The Streptomyces hemagglutinin was adsorbed to insolubilized gum arabic and eluted with 1 M NaCl containing 1 M D-galactose. The purified hemagglutinin is thought to be homogeneous judging from sodium dodecyl sulfate-polyacrylamide gel electrophoresis at pH 7.2, disc gel electrophoresis at pH 4.3, isoelectric focusing, and ultracentrifugation. The molecular weight was estimated to be 11,000 from results of gel filtration in 6 M guanidine hydrochloride (Gdn-HCl), sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and sedimentation equilibrium analysis. The amino acid analyses revealed that the hemagglutinin contained large amounts of alanine, glycine, and valine, 47% of the total amino acid residues, and no phenylalanine. Carbohydrate analysis demonstrated that the hemagglutinin might not be a glycoprotein. The circular dichroic (CD) spectrum of the protein is quite different from those of usual proteins in having a large positive peak at 226 nm (theta = 10,000) and a negative band at 212 nm (theta =-2600). The hemagglutinin showed a typical precipitation curve with gum arabic, and agglutinated human blood group B erythrocytes 256 times as strongly as A or O erythrocytes. These activities were not affected by pH (from 4 to 12). The anti-B activity was further confirmed by serological tests. The hemagglutination-inhibition studies indicated that D-galactose was inhibitory, but alpha-D-galactosides were not necessarily better inhibitors than beta-D-galactosides. L-Rhamnose was the best inhibitor among the monosaccharides tested, and L-arabinose and D-fucose were also inhibitory.

ABO Blood-Group System↗
PubMedDate not supplied

[Hemagglutinin antigens of influenza viruses isolated from man and birds].

Immunological analysis has shown hemagglutinins of avian viruses like hemagglutinins of human viruses to have a complex antigenic composition. Three antigenic determinants were discovered in hemagglutinin of A/Chicken/12/71 virus previously designated H3 and in hemagglutinin of A/Tern/18/73 virus previously designated Hav7. The H3 determinant and the second determinant are identical in avian and A/Hong Kong/1/68 human viruses. In addition, hemagglutinins of avian viruses have a determinant specific for each virus which is lacking in human influenza virus hemagglutinin.

Adsorption↗
PubMed1979

Stereochemical structure recognized by the L-fucose-specific hemagglutinin produced by Streptomyces sp.

A hemagglutinin has been purified 4000-fold from the culture filtrate of a strain of Streptomyces by affinity chromatography. The purified preparation was judged to be homogeneous by gel electrophoresis and its molecular weight was estimated to be about 70 000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis. It may exhibit its full hemagglutinating activity in the monomer form. This hemagglutinin strongly agglutinated human blood group O erythrocytes and was inhibited by L-fucose. It was, however, distinct from the known L-fucose-specific hemagglutinins; first, the hemagglutinating activity of the purified preparation was more than 100-times stronger than that of others; second, D-mannose was a potent inhibitor of this hemagglutinin besides L-fucose but not or scarcely inhibitory to others; and third, p-nitrophenyl-beta-L-fucoside was more inhibitory to this hemagglutinin than p-nitrophenyl-alpha-L-fucoside as opposed to the case of others.

ABO Blood-Group System↗
PubMed1977

Hemagglutinin-specific cytotoxic T-cell response during influenza infection.

Specific cytotoxic thymus-derived (T) lymphocytes were detected in the cervical lymph nodes and spleen during influenza infection of mice. The cytotoxic T cells can distinguish target cells infected with different influenza A subtypes. Infection with parent viruses and their recombinant progeny possessing the hemagglutinin of one parent and the neuraminidase of the other demonstrated that significant cytotoxicity occurred only when the hemagglutinin of the immunizing viruses was the same as that of the virus used to infect the target cell. In addition to this specific cytotoxic response to the major surface antigen, a cross-reactive response could be detected when the relatively nonpermissive L cell was used as the target cell. These results indicate there is a specific cytotoxic T-cell response to the surface hemagglutinin, and a cross-reactive cytotoxic response, not directed to the hemagglutinin, during influenza infection. The cytotoxic T-cell response specific for the hemagglutinin antigen may play an important role in in vivo immunity to influenza.

Animals↗
PubMed1979

Hemagglutinin mutants of swine influenza virus differing in replication characteristics in their natural host.

In two mutant clones (L and H) of A/NJ/11/76 (Hsw 1N1) influenza viruses which differ slightly antigenically and markedly in replication characteristics in chicken embryos and Madin Darby canine kidney cells, these pleiotropic differences are mediated by mutation in the hemagglutinin gene (E. D. Kilbourne, Proc. Natl. Acad. Sci. U.S.A. 75:6258--6262, 1978). Experimental infection of swine with either the mutant L and H clones or recombinant viruses differing genetically only with respect to the presence of L or H hemagglutinin demonstrated greater infectivity for the natural host of viruses bearing the L hemagglutinin. Introduction of the L but not the H hemagglutinin gene into the human influenza virus A/PR/8/34 rendered it infective for swine. Both L and H variants were isolated from pigs naturally infected with contemporary swine influenza viruses when selective conditions for the suppression of the more prevalent L mutant were employed. The L and H mutants of swine influenza virus are yet another example of viral dimorphism in nature and probably are not mere artifacts of laboratory selection. In any event, the frequent apparent allelic appearance of the two forms suggests frequent mutation and/or reversion involving a point mutation in the hemagglutinin gene. The present studies demonstrate the importance of a single gene in the pathogenesis of an influenza viral infection in its natural host.

Animals↗
PubMed1979

Live Victoria/75-ts-1[E] influenza A virus vaccines in adult volunteers: role of hemagglutinin immunity in protection against illness and infection caused by influenza A virus.

To explore the relationship between neuraminidase immunity and the degree of attenuatíon of live influenza A virus vaccines, a comparative evaluation of three Victoria/75-ts-1[E] (Vic/75-ts-1[E]) recombinant viruses in serum hemagglutination-inhibiting-negative (titer, </=1:8) adult volunteers was performed. These three ts-1[E] viruses had a similar restriction of replication at 38 degrees C in vitro, and each possessed the two attenuating genes of the ts-1[E] donor strain (13). However, Vic/75-ts-1[E] recombinants 81 and 113 possessed both Vic/75 hemagglutinin (H3(75)) and Vic/75 neuraminidase (N2(75)), whereas Vic/75-ts-1[E] recombinant 67 had Vic/75 hemagglutinin but the N2(65) neuraminidase. Vic/75-ts-1[E] recombinant 67 was significantly more attenuated than Vic/75-ts-1[E] recombinants 81 and 113 in that fewer local and systemic signs and symptoms of illness were observed in those volunteers who received clone 67. These findings were consistent with our previous observations which suggested that the following two factors contribute to the attenuation of ts-1[E] vaccine strains in adults: (i) the attenuating effect of the two ts-1[E] genes and (ii) the neuraminidase immunity of the host. Vic/75-ts-1[E] recombinant clone 67 vaccinees developed an immunological response to the H3(75) hemagglutinin in the absence of a response to the N2(75) neuraminidase. To assess the role that anti-hemagglutinin immunity induced by an attenuated live virus vaccine plays in resistance to influenza A virus, vaccinees who received recombinant 67 were challenged with Vic/75 wild-type virus, and their responses were compared with those of Vic/75-ts-1[E] vaccinees who received recombinant 81 or 113. Each of the three groups of ts-1[E] vaccinees was significantly protected against illness induced by wild-type virus infection, although resistance was not complete. However, the clone 67 vaccinees were protected less against infection. The infection-permissive resistance induced by clone 67 resembled that previously described for inactivated neuraminidase-specific vaccines. These results suggested that a ts-1[E] recombinant that possessed the hemagglutinin of a new pandemic variant, the neuraminidase of the preceding subtype, and the two ts-1[E] ts genes would be satisfactorily attenuated for children and adults with neuraminidase immunity and could induce resistance to illness caused by the new pandemic wild-type influenza A virus.

Adolescent↗
PubMed1977

Evaluation of the single radial hemolysis test for measuring hemagglutinin- and neuraminidase-specific antibodies to H3N2 influenza strains and antibodies to influenza B.

Antibodies to the H3 hemagglutinin of influenza A virus could be specifically measured by single radial hemolysis (SRH) when test antigens were recombinant viruses containing the relevant H3 hemagglutinin antigen and irrelevant Neq1 neuraminidase of A/equine/Prague/1/56 virus. Antibodies to influenza B virus could also be measured by the SRH technique. Antibody rises to influenza A or B virus measured by SRH agreed with results of hemagglutination inhibition (HI) tests for about 80% of the sera tested, including sera from volunteers receiving killed influenza vaccine and sera from patients naturally infected with influenza. Correlation between antibody titers measured by SRH and HI was also good. Antibodies to the N2 neuraminidase of influenza A virus could be specifically measured by SRH when test antigens were recombinant viruses containing the relevant N2 neuraminidase antigen and irrelevant Heq1 hemagglutinin of A/equine/Prague/1/56 virus. The SRH test for neuraminidase antibodies was more strain specific than was the SRH test for hemagglutinin antibodies. Probably for this reason, agreement between neuraminidase antibody determinations in human sera by the SRH test and by the neuraminidase inhibition test was poorer than agreement between the SRH test for hemagglutinin antibodies and the HI test.

Antibodies, Viral↗
PubMed1977

[Comparative immunochemical study of the hemagglutinins of Cl. botulinum A and B].

The authors demonstrated an incomplete indentity of Cl. botulinum hemagglutinins of types A and B in the double diffusion reaction in agar gel, and their difference by electrophoretic mobility. Some differences in the interaction of hemagglutinins A and B with human erythrocytes were found by the hemagglutination inhibition method; apparently, of the principal significance in the relization of the reaction of human erythrocyte hemagglutination with hemagglutinins of Cl. botulinum, types A and B, was the OH-group position in the C4 galactose of the mucopolysaccharides of the erythrocyte cell wall. Apart from C4, apparently, for hemagglutinin of types A of significance was the reactive capacity of C1 and C2 galactose atoms, whereas for hemagglutinin of type B--free OH-group in C2 galactose atom.

Agglutinins↗
PubMed1979

Purification of adenovirus 4 type-specific hemagglutinins for use in diagnostic counterelectrophoresis tests.

Three type-specific hemagglutinins of adenovirus (AV) 4 were purified, tested for various activities, and used as immunogens in rabbits. The components were purified by anion exchange and exclusion chromatographies to purification factors of 33, 20, and 37, respectively, and were identified as fiber (polypeptide, mol wt 70,000; incomplete hemagglutinin), penton (mol wt greater than 400,000; incomplete hemagglutinin; possession of cytotoxic activity), and dodecon (mol wt greater than 400,000; complete hemagglutinin; appearance by electron microscopy). Rabbit antisera to these hemagglutinating components possessed type-specific hemagglutination-inhibition and serum neutralization antibodies and were thoroughly evaluated for potency and specificty in immunodiffusion (ID), immunoelectrophoresis, and counterelectrophoresis (CE) tests. The anti-fiber and anti-dodecon sera were highly type-specific in ID and CE tests with a battery of commonly isolated AV serotypes; the anti-penton serum was similarly specific after it was absorbed with AV 2 hexons. These sera were thus proved to be suitable reagents for use in both the routine diagnostic ID test and the more rapid CE test.

Adenoviruses, Human↗
PubMed1979

Selective inactivation of hemagglutinin and neuraminidase on mumps virus.

The thermal stability and the effect of guanidine on the hemagglutinin and neuraminidase of three strains of mumps virus were compared. The heat inactivation of hemagglutinin resulted in the concomitant loss of neuraminidase. The effect of guanidine at various molarities showed that the neuraminidase was more sensitive than the hemagglutinin and a selective inactivation was obtained after exposure to 1.5 M guanidine. However differences in sensitivity of both activities (hemagglutinin and neuraminidase) to heat and guanidine inactivations were observed among strains and correlated with differential susceptibility to non-specific inhibitors of the strains.

Allantois↗