The structure of Sinorhizobium meliloti phage ΦM12, which has a novel T =19l triangulation number and is the founder of a new group of T4-superfamily phages

Abstract ΦM12 is the first example of a T =19l geometry capsid, encapsulating the recently sequenced genome. Here, we present structures determined by cryo-EM of full and empty capsids. The structure reveals the pattern for assembly of 1140 HK97-like capsid proteins, pointing to interactions at the...

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Published inVirology (New York, N.Y.) Vol. 450; pp. 205 - 212
Main Authors Stroupe, M. Elizabeth, Brewer, Tess E, Sousa, Duncan R, Jones, Kathryn M
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.02.2014
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Abstract Abstract ΦM12 is the first example of a T =19l geometry capsid, encapsulating the recently sequenced genome. Here, we present structures determined by cryo-EM of full and empty capsids. The structure reveals the pattern for assembly of 1140 HK97-like capsid proteins, pointing to interactions at the pseudo 3-fold symmetry axes that hold together the asymmetric unit. The particular smooth surface of the capsid, along with a lack of accessory coat proteins encoded by the genome, suggest that this interface is the primary mechanism for capsid assembly. Two-dimensional averages of the tail, including the neck and baseplate, reveal that ΦM12 has a relatively narrow neck that attaches the tail to the capsid, as well as a three-layer baseplate. When free from DNA, the icosahedral edges expand by about 5 nm, while the vertices stay at the same position, forming a similarly smooth, but bowed, T =19l icosahedral capsid.
AbstractList ΦM12 is the first example of a T=19l geometry capsid, encapsulating the recently sequenced genome. Here, we present structures determined by cryo-EM of full and empty capsids. The structure reveals the pattern for assembly of 1140 HK97-like capsid proteins, pointing to interactions at the pseudo 3-fold symmetry axes that hold together the asymmetric unit. The particular smooth surface of the capsid, along with a lack of accessory coat proteins encoded by the genome, suggest that this interface is the primary mechanism for capsid assembly. Two-dimensional averages of the tail, including the neck and baseplate, reveal that ΦM12 has a relatively narrow neck that attaches the tail to the capsid, as well as a three-layer baseplate. When free from DNA, the icosahedral edges expand by about 5nm, while the vertices stay at the same position, forming a similarly smooth, but bowed, T=19l icosahedral capsid.
Abstract ΦM12 is the first example of a T =19l geometry capsid, encapsulating the recently sequenced genome. Here, we present structures determined by cryo-EM of full and empty capsids. The structure reveals the pattern for assembly of 1140 HK97-like capsid proteins, pointing to interactions at the pseudo 3-fold symmetry axes that hold together the asymmetric unit. The particular smooth surface of the capsid, along with a lack of accessory coat proteins encoded by the genome, suggest that this interface is the primary mechanism for capsid assembly. Two-dimensional averages of the tail, including the neck and baseplate, reveal that ΦM12 has a relatively narrow neck that attaches the tail to the capsid, as well as a three-layer baseplate. When free from DNA, the icosahedral edges expand by about 5 nm, while the vertices stay at the same position, forming a similarly smooth, but bowed, T =19l icosahedral capsid.
ΦM12 is the first example of a T=19l geometry capsid, encapsulating the recently sequenced genome. Here, we present structures determined by cryo-EM of full and empty capsids. The structure reveals the pattern for assembly of 1140 HK97-like capsid proteins, pointing to interactions at the pseudo 3-fold symmetry axes that hold together the asymmetric unit. The particular smooth surface of the capsid, along with a lack of accessory coat proteins encoded by the genome, suggest that this interface is the primary mechanism for capsid assembly. Two-dimensional averages of the tail, including the neck and baseplate, reveal that ΦM12 has a relatively narrow neck that attaches the tail to the capsid, as well as a three-layer baseplate. When free from DNA, the icosahedral edges expand by about 5nm, while the vertices stay at the same position, forming a similarly smooth, but bowed, T=19l icosahedral capsid. [Display omitted] •The first T=19l geometry icosahedral bacteriophage structure is reported.•The T=19l geometry creates a quite large internal volume for packing the dsDNA genome.•ΦM12's capsid bows at the icosahedral faces when not packed with DNA, similar to other dsDNA phages.
Author Stroupe, M. Elizabeth
Sousa, Duncan R
Jones, Kathryn M
Brewer, Tess E
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Keywords ΦM12
Icosahedral
Bacteriophage
Myovirus
T=19
Sinorhizobium meliloti
Language English
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Snippet Abstract ΦM12 is the first example of a T =19l geometry capsid, encapsulating the recently sequenced genome. Here, we present structures determined by cryo-EM...
ΦM12 is the first example of a T=19l geometry capsid, encapsulating the recently sequenced genome. Here, we present structures determined by cryo-EM of full...
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SubjectTerms Amino Acid Sequence
Bacteriophage
Bacteriophage T4 - genetics
Bacteriophage T4 - isolation & purification
Bacteriophage T4 - ultrastructure
Capsid - metabolism
Capsid - ultrastructure
Capsid Proteins - chemistry
Capsid Proteins - genetics
Cryoelectron Microscopy
Icosahedral
Infectious Disease
Models, Molecular
Molecular Sequence Data
Myovirus
Sequence Alignment
Sinorhizobium meliloti
Sinorhizobium meliloti - virology
T=19
ΦM12
Title The structure of Sinorhizobium meliloti phage ΦM12, which has a novel T =19l triangulation number and is the founder of a new group of T4-superfamily phages
URI https://www.clinicalkey.es/playcontent/1-s2.0-S0042682213006399
https://dx.doi.org/10.1016/j.virol.2013.11.019
https://www.ncbi.nlm.nih.gov/pubmed/24503083
https://search.proquest.com/docview/1499125381
Volume 450
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