Evidence map›Paper›PMID 15744577›Full record

ArticleVirus genes2005

Temperature sensitive mutation in the 38 kDa minor structural protein gene of phage MB78 interferes with phage morphogenesis.

Pinaki Datta, Prabhat Mallik, Amar N Ghosh, Maharani Chakravorthy

Abstract read
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In one paragraph

Article in Virus genes, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Pinaki DattaMolecular Biology Unit, Institute of Medical Sciences, Banaras Hindu University, Varanasi, U.P., India.
Prabhat Mallik
Amar N Ghosh
Maharani Chakravorthy

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Temperature sensitive mutation in the gene for the 38 kDa minor structural protein of the phage MB78, a virulent phage of Salmonella enterica serovar typhimurium, interferes with phage development at restrictive temperature. Electron microscopy of particles produced at non-permissive temperature indicated that the particles formed are tailless. Two types of particles are seen: (i) empty capsids, which are not perfect icosahedral (ii) icosahedral particles filled with DNA. The gene for the 38 kDa protein is located in the SalIG fragment of the phage genome. Nucleotide sequence of the SalIG fragment of MB78 as well as its temperature sensitive mutant has been determined and analysed. Such analysis indicated that in the mutant the codon GCA has been changed to GTA resulting in substitution of alanine at position 75 of the protein by valine (A75V). This makes the protein thermolabile. Our results suggest that normal functioning of this 38 kDa protein is necessary for attachment of tail fibre to the capsid. Or in other words, this 38 kDa protein is involved in phage morphogenesis.

Indexed as

Genes, ViralAmino Acid SequenceAmino Acid SubstitutionBase SequenceChromosome MappingCodonDNA, ViralGenome, ViralMicroscopy, ElectronMolecular Sequence DataMolecular WeightOpen Reading FramesPoint MutationSalmonella PhagesSalmonella typhimuriumTemperatureCodonDNA, ViralViral Structural Proteins

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.