Influenza virus, hemagglutinin

Figure 5.19 Schematic picture of a single subunit of influenza virus hemagglutinin. The two polypeptide chains HAj and HA2 are held together by disulfide bridges.

Daniels, R.S., et al. Fusion mutants of the influenza virus hemagglutinin glycoprotein. Cell 40 431-439, 1985. 

Influenza virus hemagglutinin Responsible for host-cell attachment and membrane fusion... 

Fig. 76. Sialyloligosaccharide-capped carbosilane dendrimers successfully used as ligands against various strains of influenza virus hemagglutinins.433...

Okamoto S, Matsuura M, Akagi T et al (2009) Poly(y-glutamic acid) nano-particles combined with mucosal influenza virus hemagglutinin vaccine protects against influenza virus infection in mice. Vaccine 27 5896-5905... 

Fig. 4—A comparison of the H-D antigenic component and the receptor for influenza virus hemagglutinin, which are a-NeuGc-(2 — 3)-/ -Gal and a-NeuAc-(2 — 3)-/ -Gal, respectively, on the backbones / -D-Gal-( 1 — 4)-jS-d-G1cNAc-( 1 -> 3)-jS-D-Gal-(l - 4)-d-G1cNAc (sialyl i), yS-D-Gal-(l — 4)-yJ-D-GlcNAc-(l - 6)-D-Gal (sialyl I). The CH3 of the acetamido group of Ar-acetylneuraminic acid, which is a CH2OH group in iV-glycolyl-neuraminic acid, is shown.

Influenza virus hemagglutinin domain around 3-fold... 

Glyceraldehyde-phosphate dehydrogenase domain 2 Bacteriochlorophyll protein p-Hydroxybenzoate hydroxylase domain 2 Influenza virus hemagglutinin HA2 L7/L12 ribosomal protein... 

Glutathione reductase d2, d3 Influenza virus hemagglutinin HA1, HA2 p-Hydroxybenzoate hydroxylase (4-hydroxybenzoate 4-monooxygenose) dl, d2... 

Wagner E, Plank C, Zatloukal K, et al. Influenza virus hemagglutinin HA-2 N-terminal fusogenic peptides augment gene transfer by transferrin-polylysine-DNA complexes toward a synthetic virus-like gene-transfer vehicle. Proc Natl Acad Sci USA 1992 89(17) 7934-7938. 

Figure 8. Antigenic sites in the fusion region of influenza virus hemagglutinin of strains A and B. The sites have been localized and their antigenic activity confirmed by synthesis and reactivity with rabbit, goat, and mouse antivirus and antihemagglutinin antibodies. Also, each of the peptides bound considerable amounts of anti-influenza antibodies from sera of human individuals after influenza attack. Reproduced with permission from Ref. 29.

The latter approach has been followed in our laboratory. For instance, in studies related to the synthesis of potent multivalent sialoside inhibitors of influenza virus hemagglutinin [34], it became of interest to evaluate the immunogenicity of neoglycoproteins containing sialosides as sole immunodominant hapten. To this end, acetochloroneuraminic acid (1) was transformed into allyl glycoside 2 (Scheme 1) which upon reductive ozonolysis afforded aldehyde 3 in excellent overall yields [35], Reductive amination of 3 to bovine serum albumin (BSA) and tetanus toxoid provided immunogenic vaccines from which specific rabbit IgG anti-sialic acid antibodies were obtained [36]. In order... 

B pMeBHA (HF) analogues of influenza virus hemagglutinin HATU/HOAt BOP/HOBt, DIC/HOBt Kaiser test BOP/HOBt (3 equiv) in DMF, DIPEA (7.5 equiv), 2 h [370]... 

McKean, D., Huppi, K., Bell, M., Staudt, L., Gerhard, W., Weigert, M. (1984). Generation of antibody diversity in the immune response of BALB/c mice to influenza virus hemagglutinin. Proc. Natl. Acad. Sci. USA 81, 3180-3184. 

Danieli, T., Pelletier, Herds, Y.I. and White, J.M. (1996) Membrane fusion mediated by the influenza virus hemagglutinin requires the action of at least three hemagglutinin trimers. J. Cell Biol., 133, 559-569. 

Murata, M., Sugahara, Y., Takahashi, S. and Ohnishi, S. (1987) pH-dependent membrane fusion activity of a synthetic twenty amino acid peptide with the same sequence as that of the hydrophobic segment of Influenza virus hemagglutinin. J. Biochem., 102, 957-962. 

Lunn, D.P., Soboll, G., Schram, B.R., Quass, J., McGregor, M.W., Drape, R.J. etal. (1999) Antibody responses to DNA vaccination of horses using the influenza virus hemagglutinin gene. Vaccine, 17,2245-2258. 

Huang, Q., Sivaramakrishna, R. P, Ludwig, K., et al. Early steps of the conformational change of influenza virus hemagglutinin to a fusion active state Stability and energetics of the hemagglutinin. Biochim. Biophys. Acta 1614(1) 3—13. 2003. 

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