Host Range, Immunity and Antigenic Properties of Lambdoid Coliphage HK97

Dhillon, Elvera K. S.; Dhillon, T. S.; Lai, Alfred N. C.; Linn, Stuart

doi:10.1099/0022-1317-50-1-217

Cited by 27 publications

(20 citation statements)

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“…To examine these observations in detail we compare the mechanics of HK97 with that of phage λ, where no crosslinking occurs. The bacteriophages HK97 and λ are closely related in protein fold and capsid architecture (36)(37)(38). Both phages possess icosahedral shells with a T ¼ 7l triangulation number and expand during maturation to heads with approximately the same size.…”

Section: Discussionmentioning

confidence: 99%

Mechanics of bacteriophage maturation

Roos¹,

Gertsman

May

et al. 2012

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

105

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Capsid maturation with large-scale subunit reorganization occurs in virtually all viruses that use a motor to package nucleic acid into preformed particles. A variety of ensemble studies indicate that the particles gain greater stability during this process, however, it is unknown which material properties of the fragile procapsids change. Using Atomic Force Microscopy-based nano-indentation, we study the development of the mechanical properties during maturation of bacteriophage HK97, a λ-like phage of which the maturationinduced morphological changes are well described. We show that mechanical stabilization and strengthening occurs in three independent ways: (i) an increase of the Young's modulus, (ii) a strong rise of the capsid's ultimate strength, and (iii) a growth of the resistance against material fatigue. The Young's modulus of immature and mature capsids, as determined from thin shell theory, fit with the values calculated using a new multiscale simulation approach. This multiscale calculation shows that the increase in Young's modulus isn't dependent on the crosslinking between capsomers. In contrast, the ultimate strength of the capsids does increase even when a limited number of cross-links are formed while full crosslinking appears to protect the shell against material fatigue. Compared to phage λ, the covalent crosslinking at the icosahedral and quasi threefold axes of HK97 yields a mechanically more robust particle than the addition of the gpD protein during maturation of phage λ. These results corroborate the expected increase in capsid stability and strength during maturation, however in an unexpected intricate way, underlining the complex structure of these self-assembling nanocontainers.AFM | elastic network model | nanoindentation | normal mode analysis | virus structural mechanics H K97 is a double stranded DNA bacteriophage infecting Escherichia coli. The capsid protein of HK97 has a subunit fold that is shared by phages λ, P22, T4, and phi29, among others, as well as the eukaryotic virus, Herpes (1). In addition, the maturation pathways of these viruses show similar morphological changes (2). HK97 provides a unique model system to study capsid maturation, as large quantities of isometric particles can be produced in an E. coli expression system. These particles are expressed without the portal and terminase proteins used for genome packaging, but can be isolated as procapsids and matured in vitro using chemical agents instead of DNA, and maturation can be trapped in various expansion states (3, 4). In vitro expansion can be effectively induced with a variety of chemical agents, including lowering the pH below 4. The particles expand from the Prohead II (P-II) form, which differs from Prohead I (P-I) by the absence of the 104AA N-terminal polypeptide (termed the Δ-domain) from each subunit (gp5). The Δ-domain is presumed to function in scaffolding capsid assembly (5, 6). The Δ-domain is cleaved by an internally packaged protease (gp4) upon assembly, allowing the particle transition to the ...

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Section: Discussionmentioning

confidence: 99%

Mechanics of bacteriophage maturation

Roos¹,

Gertsman

May

et al. 2012

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

105

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“…1 The virus has a similar morphology to phage l, with a large icosahedral head and a long flexible tail. It belongs to the l-like genus of the siphoviridae, but the structural proteins have no detectable sequence similarity to phage l. 2 Further investigation of the structural proteins revealed significant differences in the assembly and maturation processes as compared to phage l. HK97 does not require a special scaffolding protein in assembly of the icosahedral heads, and upon maturation the gp5 proteins are covalently cross-linked throughout the head.…”

Section: Introductionmentioning

confidence: 99%

The Refined Structure of a Protein Catenane: The HK97 Bacteriophage Capsid at 3.44 Å Resolution

Helgstrand

Wikoff

Duda

et al. 2003

Journal of Molecular Biology

164

201

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“…Since many porins (OmpA, OmpF, OmpC, FhuA, and LamB) have been identified as bacteriophage receptors [5][6][7][8][20][21][22]29], and these have homologous structures [31], we can predict that analogous regions within these Omps might be globally important for phage infection. However, there are few published studies that delineate molecular mechanisms governing phage attachment to these receptors and none to date involving a member of the P22-like phages.…”

Section: Introductionmentioning

confidence: 99%

“…For example, many archaeal, eukaryotic, and bacterial viruses require proteinaceous receptors on the host surface used for attachment [2][3][4][5][6][7][8][9][10][11][12]. In addition, many of these viruses demonstrate plasticity in their binding mechanisms [3,13].…”

Section: Introductionmentioning

confidence: 99%

Key Residues of S. flexneri OmpA Mediate Infection by Bacteriophage Sf6

Porcek

Parent

2015

Journal of Molecular Biology

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Many viruses, including bacteriophage, have the inherent ability to utilize several types of proteinaceous receptors as an attachment mechanism to infect cells, yet the molecular mechanisms that drive receptor binding have not been elucidated. Using bacteriophage Sf6 and its host, Shigella flexneri, we investigated how Sf6 utilizes outer membrane protein A (OmpA) for infection. Specifically, we identified that surface loops of OmpA mediate Shigella infection. We further characterized which residues in the surface loops are responsible for Sf6 binding and productive infection using a combination of in vivo and in vitro approaches including site-directed mutagenesis, phage plaque assays, circular dichroism spectroscopy, and in vitro genome ejection assays. Our data indicate that Sf6 can productively interact with other bacterial OmpAs as long as they share homology in loops 2 and 4, suggesting that these loops may determine host specificity. Our data provide a model in which Sf6 interacts with OmpA using the surface of the protein and new insights into viral attachment through binding to membrane protein receptors.

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Host Range, Immunity and Antigenic Properties of Lambdoid Coliphage HK97

Cited by 27 publications

References 0 publications

Mechanics of bacteriophage maturation

Mechanics of bacteriophage maturation

The Refined Structure of a Protein Catenane: The HK97 Bacteriophage Capsid at 3.44 Å Resolution

Key Residues of S. flexneri OmpA Mediate Infection by Bacteriophage Sf6

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