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Role of SH3b binding domain in a natural deletion mutant of Kayvirus endolysin LysF1 with a broad range of lytic activity

Overview of attention for article published in Virus Genes, August 2017
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About this Attention Score

  • Above-average Attention Score compared to outputs of the same age (62nd percentile)
  • Good Attention Score compared to outputs of the same age and source (77th percentile)

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Citations

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52 Mendeley
Title
Role of SH3b binding domain in a natural deletion mutant of Kayvirus endolysin LysF1 with a broad range of lytic activity
Published in
Virus Genes, August 2017
DOI 10.1007/s11262-017-1507-2
Pubmed ID
Authors

Martin Benešík, Jiří Nováček, Lubomír Janda, Radka Dopitová, Markéta Pernisová, Kateřina Melková, Lenka Tišáková, Jiří Doškař, Lukáš Žídek, Jan Hejátko, Roman Pantůček

Abstract

The spontaneous host-range mutants 812F1 and K1/420 are derived from polyvalent phage 812 that is almost identical to phage K, belonging to family Myoviridae and genus Kayvirus. Phage K1/420 is used for the phage therapy of staphylococcal infections. Endolysin of these mutants designated LysF1, consisting of an N-terminal cysteine-histidine-dependent aminohydrolase/peptidase (CHAP) domain and C-terminal SH3b cell wall-binding domain, has deleted middle amidase domain compared to wild-type endolysin. In this work, LysF1 and both its domains were prepared as recombinant proteins and their function was analyzed. LysF1 had an antimicrobial effect on 31 Staphylococcus species of the 43 tested. SH3b domain influenced antimicrobial activity of LysF1, since the lytic activity of the truncated variant containing the CHAP domain alone was decreased. The results of a co-sedimentation assay of SH3b domain showed that it was able to bind to three types of purified staphylococcal peptidoglycan 11.2, 11.3, and 11.8 that differ in their peptide bridge, but also to the peptidoglycan type 11.5 of Streptococcus uberis, and this capability was verified in vivo using the fusion protein with GFP and fluorescence microscopy. Using several different approaches, including NMR, we have not confirmed the previously proposed interaction of the SH3b domain with the pentaglycine bridge in the bacterial cell wall. The new naturally raised deletion mutant endolysin LysF1 is smaller than LysK, has a broad lytic spectrum, and therefore is an appropriate enzyme for practical use. The binding spectrum of SH3b domain covering all known staphylococcal peptidoglycan types is a promising feature for creating new chimeolysins by combining it with more effective catalytic domains.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 52 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 52 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 8 15%
Researcher 8 15%
Professor > Associate Professor 6 12%
Student > Master 5 10%
Student > Doctoral Student 2 4%
Other 5 10%
Unknown 18 35%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 13 25%
Agricultural and Biological Sciences 8 15%
Immunology and Microbiology 5 10%
Engineering 2 4%
Medicine and Dentistry 2 4%
Other 2 4%
Unknown 20 38%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 4. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 17 August 2022.
All research outputs
#7,328,780
of 23,106,934 outputs
Outputs from Virus Genes
#169
of 978 outputs
Outputs of similar age
#115,679
of 316,140 outputs
Outputs of similar age from Virus Genes
#4
of 18 outputs
Altmetric has tracked 23,106,934 research outputs across all sources so far. This one has received more attention than most of these and is in the 67th percentile.
So far Altmetric has tracked 978 research outputs from this source. They receive a mean Attention Score of 2.4. This one has done well, scoring higher than 81% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 316,140 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 62% of its contemporaries.
We're also able to compare this research output to 18 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 77% of its contemporaries.