Assembly and Maturation of the Bacteriophage Lambda Procapsid: gpC Is the Viral Protease

Medina, E; Wieczorek, Doug; Medina, Eva M.; Yang, Qin; Feiss, Michael; Catalano, Carlos Enrique

doi:10.1016/j.jmb.2010.06.060

Cited by 34 publications

(42 citation statements)

References 48 publications

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“…In phage HK97, the gp4 uncleaved protease stabilizes the initial procapsid prior to autoproteolysis and digestion of the scaffolding domain of the major head protein gp5 (63). In phage , the gpC protease degrades the scaffolding protein gpNu3 and cleaves the N-terminal end of the portal protein gpB (64). For both phages, the digested proteases escape the capsid before or upon DNA packaging.…”

Section: Discussionmentioning

confidence: 99%

Insights into Bacteriophage T5 Structure from Analysis of Its Morphogenesis Genes and Protein Components

Zivanovic

Confalonieri

Ponchon

et al. 2014

J Virol

104

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Bacteriophage T5 represents a large family of lytic Siphoviridae infecting Gram-negative bacteria. The low-resolution structure of T5 showed the T‫31؍‬ geometry of the capsid and the unusual trimeric organization of the tail tube, and the assembly pathway of the capsid was established. Although major structural proteins of T5 have been identified in these studies, most of the genes encoding the morphogenesis proteins remained to be identified. Here, we combine a proteomic analysis of T5 particles with a bioinformatic study and electron microscopic immunolocalization to assign function to the genes encoding the structural proteins, the packaging proteins, and other nonstructural components required for T5 assembly. A head maturation protease that likely accounts for the cleavage of the different capsid proteins is identified. Two other proteins involved in capsid maturation add originality to the T5 capsid assembly mechanism: the single head-to-tail joining protein, which closes the T5 capsid after DNA packaging, and the nicking endonuclease responsible for the single-strand interruptions in the T5 genome. We localize most of the tail proteins that were hitherto uncharacterized and provide a detailed description of the tail tip composition. Our findings highlight novel variations of viral assembly strategies and of virion particle architecture. They further recommend T5 for exploring phage structure and assembly and for deciphering conformational rearrangements that accompany DNA transfer from the capsid to the host cytoplasm. Bacteriophage T5 is a member of the Siphoviridae family infecting Escherichia coli. It consists of an icosahedral capsid containing a large molecule of double-stranded DNA (dsDNA) (121.75 kbp) attached to a long flexible noncontractile tail. The complete genomes of two wild-type T5 strains (GenBank accession numbers AY587007 [1] and AY543070) and of the heat-stable deletion mutant T5st0 (GenBank accession number AY692264 [this study]) have been sequenced. Moreover, the genomes of T5-related phages H8 (2), EPS7 (3), SPC35 (4), AKVF3 (5), pVp-1 (6), and My1 (7) exhibit high sequence similarity to T5. Of the 159 to 174 genes predicted in each genome, about 70 were assigned functions on the basis of similarity searches and/or previous genetic studies. Most of the identified genes are related to nucleotide metabolism, DNA replication, recombination, and various enzymatic functions. Despite the fact that the major structural proteins of T5 have been identified (8), the functions of 13 of the 23 late genes encoding the structural and morphogenesis proteins remain to be ascertained.The overall structure of T5 was solved by cryo-electron microscopy (cryo-EM) and image reconstruction (9). The large icosahedral capsid consists of the coat protein pb8, arranged as 11 pentamers at the vertices and 120 hexamers on the faces. The 12th vertex is occupied by a dodecamer of the portal protein pb7. The early events of T5 capsid assembly have been partly deciphered (10). The initial shell (prohead I) is assemb...

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Section: Discussionmentioning

confidence: 99%

Insights into Bacteriophage T5 Structure from Analysis of Its Morphogenesis Genes and Protein Components

Zivanovic

Confalonieri

Ponchon

et al. 2014

J Virol

104

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“…The recycled P22 scaffolding protein can be reused four more times in the assembly process [109]. Lambda scaffolding protein can also exit from the capsid without being cleaved, as was shown for the phage with a genetically inactivated protease [110]. The release of scaffolding proteins could be induced by their interaction with DNA, possibly through a leucine-zipper motif, identified in the scaffolding protein of phi29 [58].…”

Section: Dsdna Tailed Phagesmentioning

confidence: 99%

Bacteriophage Assembly

Aksyuk

Rossmann

2011

Viruses

123

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Bacteriophages have been a model system to study assembly processes for over half a century. Formation of infectious phage particles involves specific protein-protein and protein-nucleic acid interactions, as well as large conformational changes of assembly precursors. The sequence and molecular mechanisms of phage assembly have been elucidated by a variety of methods. Differences and similarities of assembly processes in several different groups of bacteriophages are discussed in this review. The general principles of phage assembly are applicable to many macromolecular complexes.

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“…Briefly, assembly initiates with self-association of the portal protein (gpB) into a dodecameric ring structure. [12][13][14][15] This nucleates polymerization of the major capsid protein (gpE) into an icosahedral shell, chaperoned by co-polymerization with the scaffolding protein (gpNu3). [16][17][18][19] A limited number of viral protease proteins (gpC) are also incorporated into the nascent procapsid interior, which auto digests, degrades the scaffold protein, and removes 20 residues from the N-terminus of roughly half of the portal proteins.…”

Section: Introductionmentioning

confidence: 99%

“…[16][17][18][19] A limited number of viral protease proteins (gpC) are also incorporated into the nascent procapsid interior, which auto digests, degrades the scaffold protein, and removes 20 residues from the N-terminus of roughly half of the portal proteins. 13,14 The proteolysis products exit the structure to afford the mature procapsid composed of a portal ring situated at a unique vertex of the icosahedral shell; this portal vertex provides a hole through which viral DNA can enter during packaging and exit during infection.…”

Section: Introductionmentioning

confidence: 99%

Thermodynamic Characterization of Viral Procapsid Expansion into a Functional Capsid Shell

Medina

Nakatani

Kruse

et al. 2012

Journal of Molecular Biology

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Assembly and Maturation of the Bacteriophage Lambda Procapsid: gpC Is the Viral Protease

Cited by 34 publications

References 48 publications

Insights into Bacteriophage T5 Structure from Analysis of Its Morphogenesis Genes and Protein Components

Insights into Bacteriophage T5 Structure from Analysis of Its Morphogenesis Genes and Protein Components

Bacteriophage Assembly

Thermodynamic Characterization of Viral Procapsid Expansion into a Functional Capsid Shell

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