Roles of pIII in filamentous phage assembly

Rakonjac, Jasna; Model, Peter

doi:10.1006/jmbi.1998.2006

Cited by 73 publications

(79 citation statements)

References 44 publications

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“…3, B and C). The U-shaped N-terminal loop that lies at the bottom of the ␤-barrel is followed by its first ␤-strand, ␤1 (residues [13][14][15][16][17]. From ␤1 the polypeptide chain crosses the top of the ␤-barrel to form ␤2 (26 -29) on its opposite side.…”

Section: Resultsmentioning

confidence: 99%

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Crystal Structures of a CTXφ pIII Domain Unbound and in Complex with a Vibrio cholerae TolA Domain Reveal Novel Interaction Interfaces

Ford

Kolappan

Phan

et al. 2012

Journal of Biological Chemistry

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Background: CTX infection of Vibrio cholerae confers toxigenicity. Results: We report crystal structures of CTX-pIII domain N1 alone and bound to V. cholerae TolA domain C. Conclusion: CTX and coliphage pIII use distinct mechanisms to bind to TolA. Significance: These structures contribute to our understanding of a critical step in the evolution of pandemic V. cholerae with implications for emerging V. cholerae pathogens.

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Section: Resultsmentioning

confidence: 99%

“…Although pVI and pI are very small, pIII is a large protein, present in four-five copies at one end of the phage particle. pIII (also called g3p for gene 3 protein) mediates phage binding, uptake, and assembly (15)(16)(17)(18)(19).…”

mentioning

confidence: 99%

Crystal Structures of a CTXφ pIII Domain Unbound and in Complex with a Vibrio cholerae TolA Domain Reveal Novel Interaction Interfaces

Ford

Kolappan

Phan

et al. 2012

Journal of Biological Chemistry

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“…Similarly, other alternative phage recovery processes, such as low pH acid elution or DTT treatment, which also have no effect on wild-type phage, may have adverse effects on some fraction of the members of a particular library, a fact that cannot be predicted in advance. The N-terminal domain of pIII is required for phage infectivity by attachment to the tip of the FЈ pilus of E. coli, whereas the C-terminal portion of pIII acts in combination with pVI to cap the trailing end of the filament during phage assembly, allowing its release from the cell (59). A potential advantage of pIXdisplay is that elution is not necessary to rescue phages that specifically bind to immobilized targets.…”

Section: Discussionmentioning

confidence: 99%

A method for the generation of combinatorial antibody libraries using pIX phage display

Gao

Mao

Kaufmann

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

117

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For more than a decade, phage displayed combinatorial antibody libraries have been used to generate and select a wide variety of antibodies. We previously reported that the phage coat proteins pVII and pIX could be used to display the heterodimeric structure of the antibody Fv region. Herein, aspects of this technology were invoked and extended to construct a large, human single-chain Fv (scFv) library of 4.5 ؋ 10 9 members displayed on pIX of filamentous bacteriophage. Furthermore, the diversity, quality, and utility of the library were demonstrated by the selection of scFv clones against six different protein antigens. Notably, more than 90% of the selected clones showed positive binding for their respective antigens after as few as three rounds of panning. Analyzed scFvs were also found to be of high affinity. For example, kinetic analysis (BIAcore) revealed that scFvs against staphylococcal enterotoxin B and cholera toxin B subunit had a nanomolar and subnanomolar dissociation constant, respectively, affording affinities comparable to, or exceeding that, of mAbs obtained from immunization. High specificity was also attained, not only between very distinct proteins, but also in the case of the Ricinus communis (''ricin'') agglutinins (RCA60 and RCA120), despite >80% sequence homology between the two. The results suggested that the performance of pIX-display libraries can potentially exceed that of the pIII-display format and make it ideally suited for panning a wide variety of target antigens.

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“…This hypothesis was tested by infecting cells with III Ϫ IV Ϫ phage that make neither pIV nor pIII. In the absence of pIII, phage particles are assembled and exported across the outer membrane, but they remain attached to the cell surface (4). The number of phage exported (in phage genomes) is similar to that in wild-type infected cells, and the physiology of the infected cells is unchanged.…”

Section: Resultsmentioning

confidence: 99%

“…When the entire DNA molecule has been coated and extruded, two other minor proteins, pIII and pVI, are added to the end of the virion (3). pIII and pVI are necessary to release the phage from the cell; in their absence, very long phage that contain multiple unit-length phage genomes are produced and remain attached to the cell surface (4,5).…”

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confidence: 99%

Assembling filamentous phage occlude pIV channels

Marciano

Russel

Simon

2001

Proc. Natl. Acad. Sci. U.S.A.

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Filamentous phage f1 is exported from its Escherichia coli host without killing the bacterial cell. Phage-encoded protein pIV, which is required for phage assembly and secretion, forms large highly conductive channels in the outer membrane of E. coli. It has been proposed that the phage are extruded across the bacterial outer membrane through pIV channels. To test this prediction, we developed an in vivo assay by using a mutant pIV that functions in phage export but whose channel opens in the absence of phage extrusion. In E. coli lacking its native maltooligosacharride transporter LamB, this pIV variant allowed oligosaccharide transport across the outer membrane. This entry of oligosaccharide was decreased by phage production and still further decreased by production of phage that cannot be released from the cell surface. Thus, exiting phage block the pIV-dependent entry of oligosaccharide, suggesting that phage occupy the lumen of pIV channels. This study provides the first evidence, to our knowledge, for viral exit through a large aqueous channel.

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Roles of pIII in filamentous phage assembly

Cited by 73 publications

References 44 publications

Crystal Structures of a CTXφ pIII Domain Unbound and in Complex with a Vibrio cholerae TolA Domain Reveal Novel Interaction Interfaces

Crystal Structures of a CTXφ pIII Domain Unbound and in Complex with a Vibrio cholerae TolA Domain Reveal Novel Interaction Interfaces

A method for the generation of combinatorial antibody libraries using pIX phage display

Assembling filamentous phage occlude pIV channels

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