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Titolo:
STRUCTURAL CONSTRAINTS ON THE DISPLAY OF FOREIGN PEPTIDES ON FILAMENTOUS BACTERIOPHAGES
Autore:
MAKOWSKI L;
Indirizzi:
FLORIDA STATE UNIV,INST MOLEC BIOPHYS TALLAHASSEE FL 32306
Titolo Testata:
Gene
fascicolo: 1, volume: 128, anno: 1993,
pagine: 5 - 11
SICI:
0378-1119(1993)128:1<5:SCOTDO>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
COAT PROTEIN; NEUTRON-DIFFRACTION; FD; DNA; PFL;
Keywords:
DISPLAY VECTORS; VIRUS STRUCTURE AND ASSEMBLY; ESCHERICHIA-COLI PHAGE-M-13; PSEUDOMONAS PHAGE-PF-1; X-RAY DIFFRACTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
L. Makowski, "STRUCTURAL CONSTRAINTS ON THE DISPLAY OF FOREIGN PEPTIDES ON FILAMENTOUS BACTERIOPHAGES", Gene, 128(1), 1993, pp. 5-11

Abstract

Strategies for the construction of vehicles for phage display are evaluated here on the basis of structural studies of filamentous bacteriophages. Potential sites for the insertion of foreign peptides into themajor coat protein, gp8, of M 13 are identified. Currently, the insertion of peptides into gp8 has two basic limitations: all insertion sites that have been used successfully are located within 5 amino acids (aa) of the N terminus, and in virions containing only mutant coat proteins, insertions larger than about 6 aa have not been successfully incorporated. The possible reasons for these limitations are discussed interms of the structures of gp8 and the minor structural proteins, gp7and gp9. Potential strategies for overcoming these limitations are outlined. Reasons for the successful incorporation of larger inserts into hybrid phage containing both native and mutant coat proteins are also discussed. The structures of gp6, gp7, and gp9 are described, and itis concluded that insertion sites in these minor proteins are unlikely to have substantial advantages over those currently being used in gp3. The structure of the coat protein of another filamentous phage, Pseudomonas phage Pf1, is also described. Its structure provides a numberof clues for the successful design of phage display insertion sites. Because it contains a 7-aa surface loop in the major coat protein, thePf1 coat protein may have significant advantages over gp8 of M 13 as a vehicle for phage display.

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Documento generato il 01/12/20 alle ore 10:34:12