Interaction of the globular domains of pill protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli

Virology

Volumn 253, Issue 2, 1999, Pages 271-277

  Deng, Lih Wen ^a   Malik, Pratap ^a,b   Perham, Richard N ^a,b  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN;

ARTICLE; BACTERIOPHAGE; ESCHERICHIA COLI; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; VIRUS CELL INTERACTION;

ENTEROBACTERIA PHAGE FD; ESCHERICHIA COLI; FILAMENTOUS BACTERIOPHAGE; NEGIBACTERIA;

EID: 0033585380     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9509     Document Type: Article

References (36)

1. Armstrong, J., Perham, R. N., and Walker, J. E. (1981). Domain structure of bacteriophage fd adsorption protein. FEBS Lett. 135, 167-172.
2. Boeke, J. D., Model, P., and Zinder, N. D. (1982). Effects of bacteriophage f1 gene III protein on the host cell membrane. Mol. Gen. Genet. 186, 185-192.
3. Cortese, R., Monaci, P., Luzzago, A., Santini, C., Bartoli, F., Cortese, I., Fortugno, P., Galfre, G., Nicosia, A., and Felici, F. (1996). Selection of biologically active peptides by phage display of random peptide libraries. Curr. Opin. Biotechnol. 7, 616-621.
4. Crissman, J. W., and Smith, G. P. (1984). Gene III protein of filamentous phages: Evidence for a carboxyl-terminal domain with a role in morphogenesis. Virology 132, 445-455.
5. Date, T., Goodman, J., and Wickner, W T. (1980). Procoat, the precursor of M13 coat protein, requires an electrochemical potential for membrane insertion. Proc. Natl. Acad. Sci. USA 77, 4669-4673.
6. Davis, N. G., Boeke, J. D., and Model, P. (1985). Fine structure of a membrane anchor domain. J. Mol. Biol. 181, 111-121.
7. Gallusser, A., and Kuhn, A. (1990). Initial steps in protein membrane insertion: Bacteriophage M13 procoat protein binds to the membrane surface by electrostatic interaction. EMBO J. 9, 2723-2729.
8. Glaserwuttke, G., Keppner, J., and Rasched, I. (1989). Pore forming properties of the adsorption protein of filamentous phage fd. Biochim. Biophys. Acta 985, 239-247.
9. Gray, C. W., Brown, R. S., and Marvin, D. A. (1981). Adsorption complex of filamentous fd virus. J. Mol. Biol. 146, 621-627.
10. Hawkins, C. F., Borges, A., and Perham, R. N. (1990). Cloning and sequence analysis of the genes encoding the α and β subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of bacillus stearothermophilus. Eur. J. Biochem. 191, 337-346.
11. Hochuli, E., Bannwarth, W., Dobeli, H., Gentz, R., and Stuber, D. (1988). Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent. Biotechnology 6, 1321-1325.
12. Holliger, P., and Riechmann, L. (1997). A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd. Structure 5, 265-275.
13. Jacobson, A. (1972). Role of F-pili in the penetration of bacteriophage f1. J. Virol. 10, 835-843.
14. Jelinek, R., Terry, T. D., Gesell, J. J., Malik, P., Perham, R. N., and Opella, S. J. (1997). NMR structure of the principal neutralizing determinant of HIV-1 displayed in filamentous bacteriophage coat protein. J. Mol. Biol. 266, 649-655.
15. Kay, B. K., and Paul, J. I. (1996). High throughput screening strategies to identify inhibitors of protein-protein interactions. Mol. Div. 1, 139-140.
16. Kremser, A., and Rasched, I. (1994). The adsorption protein of filamentous phage fd: Assignment of its disulfide bridges and identification of the domain incorporated in the coat. Biochemistry 33, 13954-13958.
17. Kuhn, A. (1987). Bacteriophage M13 procoat protein inserts into the plasma membrane as a loop structure. Science 238, 1413-1415.
18. Kuhn, A., Kreil, G., and Wickner, W. (1987). Recombinant forms of M13 procoat with an ompa leader sequence or a large carboxy-terminal extension retain their independence of secy function. EMBO J. 6, 501-505.
19. Lubkowski, J., Hennecke, F., Plückthun, A., and Wlodawer, A. (1998). The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p. Nature Struct. Biol. 5, 140-147.
20. Malik, P., and Perham, R. N. (1996). New vectors for peptide display on the surface of filamentous bacteriophage. Gene 171, 49-51.
21. Malik, P., Terry, T. D., and Perham, R. N. (1996). Mutiple display of foreign peptide epitopes on filamentous bacteriophage virions. In "Phage Display of Peptides and Proteins: A Laboratory Manual" (B. K. Kay, J. Winter, and J. McCafferty Eds.), pp. 127-139. Academic Press, San Diego.
22. Marvin, D. A., and Hohn, B. (1969). Filametous bacterial viruses. Bacteriol. Rev. 33, 172-209.
23. Model, P., and Russel, M. (1988). Filamentous bacteriophage. In "The Bacteriophages" (R. Calendar, Ed.), pp. 375-456. Plenum, New York.
24. Perham, R. N., Terry, T. D., Willis, A. E., Greenwood, J., Veronese, F. D., and Appella, E. (1995). Engineering a peptide epitope display system on filamentous bacteriophage. FEMS Microbiol. Rev. 17, 25-31.
25. Peters, E. A., Schatz, P. J., Johnson, S. S., and Dower, W. J. (1994). Membrane insertion defects caused by positive charges in the early mature region of protein pIII of filamentous phage fd can be corrected by prlA suppressors. J. Bacteriol. 176, 4296-4305.
26. Rampf, B., Bross, P., Vocke, T., and Rasched, I. (1991). Release of periplasmic proteins induced in escherichia coli by expression of an N-terminal proximal segment of the phage fd gene 3 protein. FEBS Lett. 280, 27-31.
27. Rasched, I., and Oberer, E. (1986). Ff coliphages: Structural and functional relationships. Microbiol. Rev. 50, 401-427.
28. Reche, P., Li, Y. L., Fuller, C., Eichhorn, K., and Perham, R. N. (1998). Selectivity of posttranslational modification in biotinylated proteins: The carboxy carrier protein of the acetyl-CoA carboxylase of escherichia coli. Biochem. J. 329, 589-596.
29. Ricaud, P. M., Howard, M. J., Robers, E. M., Broadhurst, R. W., and Perham, R. N. (1996). Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of escherichia coli. J. Mol. Biol. 264, 179-190.
30. Riechmann, L., and Holliger, P. (1997). The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. Coli. Cell 90, 351-360.
31. Sambrook, J., Fritsh, E. F., and Maniatis, T. (1989). "Molecular Cloning: A Laboratory Manual." Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
32. Smith, G. P., and Scott, J. K. (1993). Libraries of peptides and proteins displayed on filamentous phage. Methods Enzymol. 217, 228-257.
33. Stengele, I., Bross, P., Garces, X., Giray, J., and Rasched, I. (1990). Dissection of functional domains in phage fd adsorption protein: Discrimination between attachment and penetration sites. J. Mol. Biol. 212, 143-149.
34. Sun, T. P., and Webster, R. E. (1987). Nucleotide sequence of a gene cluster involved in entry of E colicins and single-stranded DNA of infecting filamentous bacteriophages into escherichia coli. J. Bacteriol. 169, 2667-2674.
35. Winter, G., Griffiths, A. D., Hawkins, R. E., and Hoogenboom, H. R. (1994). Making antibodies by phage display technology. Annu. Rev. Immunol. 12, 433-455.
36. Yanischperron, C., Vieira, J., and Messing, J. (1985). Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119.