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 in | Virology (New York, N.Y.) Vol. 450; pp. 205 - 212 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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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. |
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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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CitedBy_id | crossref_primary_10_3389_fmicb_2020_00022 crossref_primary_10_1128_spectrum_02827_23 crossref_primary_10_1016_j_csbj_2021_12_032 crossref_primary_10_1073_pnas_1807706115 crossref_primary_10_1099_jgv_0_001487 crossref_primary_10_1016_j_jsb_2017_08_005 crossref_primary_10_1128_JVI_01875_14 crossref_primary_10_1128_mBio_01579_17 crossref_primary_10_1128_JVI_01353_15 crossref_primary_10_1016_j_virol_2015_02_055 crossref_primary_10_1099_mgen_0_001063 crossref_primary_10_1128_JVI_01356_21 crossref_primary_10_3390_microorganisms8121944 |
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Keywords | ΦM12 Icosahedral Bacteriophage Myovirus T=19 Sinorhizobium meliloti |
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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 |
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