Interactions of phage P22 tails with their cellular receptor, Salmonella O-antigen polysaccharide

Biophysical Journal

Volumn 71, Issue 4, 1996, Pages 2040-2048

  Baxa, Ulrich ^a   Steinbacher, Stefan ^b   Miller, Stefan ^a,d   Weintraub, Andrej ^c   Huber, Robert ^b   Seckler, Robert ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^c KAROLINSKA UNIVERSITY HOSPITAL   (Sweden)

^d MAX PLANCK INST FÜR BIOLOGIE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGE DNA; DODECASACCHARIDE; ENDORHAMNOSIDASE; O ANTIGEN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GROWTH; BACTERIOPHAGE; BINDING KINETICS; CARBOHYDRATE SYNTHESIS; ENZYME SUBUNIT; MOLECULAR RECOGNITION; PROTEIN PROTEIN INTERACTION; REACTION TIME; RECEPTOR BINDING; SALMONELLA;

BACTERIA (MICROORGANISMS); ENTERITIDIS; SALMONELLA; SALMONELLA ENTERITIDIS; SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0029816431     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79402-X     Document Type: Article

References (33)

1. Bayer, M. E., K. Takeda, and H. Uetake. 1980. Effects of receptor destruction by Salmonella bacteriophages ∈15 and c341. Virology. 105: 328-337.
2. Berget, P. B., and A. R. Poteete. 1980. Structure and function of the bacteriophage P22 tail protein. J. Virol. 34:234-243.
3. Dandliker, W. B., M.-L. Hsu, J. Levin, and B. R. Rao. 1981. Equilibrium and kinetic inhibition assays based upon fluorescence polarization. Methods Enzymol. 74:3-28.
4. Danner, M., A. Fuchs, S. Miller, and R. Seckler. 1993. Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal head-binding domain. Eur. J. Biochem. 215:653-661.
5. Eriksson, U., S. B. Svenson, J. Lönngren, and A. A. Lindberg. 1979. Salmonella phage glycanases: substrate specificity of the phage P22 endo-rhamnosidase. J. Gen. Virol. 43:503-511.
6. Frieden, C. 1994. Numerical integration of rate equations by computer: an update. Trends Biochem. Sci. 19:181-182.
7. Fuchs, A., C. Seiderer, and R. Seckler. 1991. In vitro folding pathway of the P22 tailspike protein. Biochemistry. 30:6598-6604.
8. Goldenberg, D., and J. King. 1982. Trimeric intermediate in the in vivo folding and assembly of the tail spike endorhamnosidase of bacteriophage P22. Proc: Natl. Acad. Sci. USA. 79:3403-3407.
9. Herrler, G., H.-J. Gross, A. Imhof. R. Brossmer, G. Milks, and J. C. Paulson. 1992. A synthetic sialic acid analogue is recognized by Influenza C virus as a receptor determinant but is resistant to the receptor-destroying enzyme. J. Biol. Chem. 267:12501-12505.
10. Huberman, K., R. W. Peluso, A. Moscona 1995. Hemagglutininneuraminidase of human paraintluenza 3: role of the neuraminidase in the viral life cycle. Virology. 214:294-300.
11. Israel, J. V., T. F. Anderson, and M. Levine. 1967. In vitro morphogenesis of phage P22 from heads and base-plate parts. Proc. Natl. Acad. Sci. USA. 57:284-291.
12. Israel, V. 1978. A model for the adsorption of phage P22 to Salmonella typhimurium. J. Gen. Virol. 40:669-673.
13. Iwashita, S., and S. Kanegasaki. 1976a. Enzymic and molecular properties of base-plate parts of bacteriophage P22. Eur. J. Biochem. 65:87-94.
14. Iwashita, S., and S. Kanegasaki. 1976h. Deacetylation reaction catalyzed by Salmonella phage c341 and its baseplate parts. J. Biol. Chem. 251: 5361-5365.
15. Kanaoka, Y., T. Takahashi, H. Nakayama, and K. Tanizawa. 1985. New fluorogenic substrates for subtilisin. Chem. Pharm. Bull. (Tokyo). 33: 1721-1724.
16. Koshland, D. E. 1953. Stereochemistry and mechanism of enzymatic reactions. Biol. Rev. 28:416-436.
17. Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
18. Lentz, T. L. 1990. The recognition event between virus and host cell receptor: a target for antiviral agents. J. Gen. Virol. 71:751-766.
19. Lindberg, A. A. 1977. Bacterial surface carbohydrates and bacteriophage adsorption. In Surface Carbohydrates of the Procaryotic Cell. I. W. Sutherland, editor. Academic Press, London, 289-356.
20. Liu, C., M. C. Eichelberger, R. W. Compans, and G. M. Air. 1995. Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J. Virol. 69:1099-1106.
21. Miller, S. 1995. Deletions- und Punktmutanten des P22-Tailspike-Proteins: Klonierung, Reinigung, Kristallisation und Physikalisch-Biochemische Analyse. Thesis, Universität Regensburg, Regensberg, Germany.
22. Prakash, C., and I. K. Vijai. 1983. A new fluorescent tag for labeling of saccharides. Anal. Biochem. 128:41-46.
23. Schwarz, J. J., and P. B. Berget. 1989. Characterization of bacteriophage P22 tailspike mutants with altered endorhamnosidase and capsid assembly activities. J. Biol. Chem. 264:20112-20119.
24. Seckler, R., A. Fuchs, J. King, and R. Jaenicke. 1989. Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro. J. Biol. Chem. 264:11750-11753.
25. Sigurskjold, B. W., and D. R. Bundle. 1992. Thermodynamics of oligosaccharide binding to a monoclonal antibody specific for a Salmonella O-antigen point to hydrophobic interactions in the binding site. J. Biol. Chem. 267:8371-8376.
26. Spolar, R. S., and M. T. Record, Jr. 1994. Coupling of local folding to site-specific binding of proteins to DNA. Science. 263:777-784.
27. Steinbacher, S., R. Seckler, S. Miller, B. Steipe, R. Huber, and P. Reinemer. 1994. Crystal structure of P22 tailspike-protein. Interdigitated subunits in a thermostable trimer. Science. 265:383-386.
28. Svenson, S. B., J. Lönngren, N. Carlin, and A. A. Lindberg. 1979. Salmonella bacteriophage glycanases: endorhamnosidases of Salmonella typhimurium bacteriophages. J. Virol. 32:583-592.
29. Vyas, N. K. 1991. Atomic features of protein-carbohydrate interactions. Curr. Opin. Struct. Biol. 1:732-740.
30. Weintraub, A., A. A. Lindberg, P. Lipniunas, and B. Nilsson. 1988. Heterogeneity of oligosaccharides from the O-polysaccharide chain of the lipopolysaccharide from Salmonella typhi 253Ty determined by fast atom bombardment mass spectrometry. Glycoconj. J. 5:207-213.
31. Withers, S. G., and R. Aebershold. 1995. Approaches to labeling and idenfication of active site residues in glycosidases. Protein Sci. 4:361-372.
32. Yuckenberg, P. D., F. Witney, J. Geisselsoder, and J. McClary. 1991. Site-directed in vitro mutagenesis using uracil-containing DNA and phagemid vectors. In Directed Mutagenesis, A Practical Approach. M. J. MacPherson, editor. IRL Press, Oxford. 27-48.
33. Zidovetzki, R., Y. Blatt, G. Schepers, and I. Pecht. 1988. Thermodynamics of oligosaccharides binding to a dextran-specific monoclonal IgM. Mol. Immunol. 25:379-383.