ArticleBMC microbiology2026
Impairment of two non-essential LytR-cpsA-psr (Lcp) cell wall ligases decelerate cell wall assembly in Mycolicibacterium smegmatis.
Article in BMC microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
backgroundThe LytR-CpsA-Psr (Lcp) family of proteins are highly abundant amongst actinomycetes and Gram-positive bacteria, and known to exist as multiple paralogs in an organism. Several reports demonstrated the essential LcpA to play a crucial role in coupling cell wall teichoic acids (arabinogalactan in mycobacteria) to peptidoglycan, making it an attractive drug target against tuberculosis (TB). However, apart from LcpB that accommodates capsular biosynthesis, role of the non-essential Lcp paralogs in mycobacteria largely remains elusive. Therefore, we made a comprehensive approach in characterizing the role of these non-essential Lcp proteins in mycobacterial cell wall assembly. Additionally, we used homology and interactive models as an alternate approach to X-ray crystallography, to identify hotspot residues for Lcp inhibition and subsequent bactericidal activity.
resultsSingle and double knockout strains of each of the three Mycolicibacterium smegmatis (M. smegmatis) non-essential lcp genes were generated, out of which ΔlcpBΔlcpC exhibited severely compromised cell envelope with impeding cell division, altered morphology, reduced biofilms, enhanced susceptibility to stress, loss of capsular ⍺-glucans and exposed Galf residues. The higher pyrophosphatase activity of LcpB and LcpC, their interaction in native conditions and reduced AG/PG markers in ΔlcpBΔlcpC, substantiates their role in AG-PG ligation. Higher expression of lcpB/lcpC irrespective of external stress indicates tight regulation and coping mechanism conferred by these two homologs on the mycobacterial cell. Cell wall targeting anti-TB drugs in combination with two Lcp inhibitory compounds, Entrectinib and Sorafenib, proved bactericidal.
conclusionThis study highlights the primary role of LcpB/LcpC alongside LcpA in maintaining structural integrity of the M. smegmatis cell envelope, and combined anti-Lcp drug strategy as a novel approach to inhibit mycobacterial replication.
Indexed as
Identifiers
What Socratic holds
Registered trials
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 Socratic graph.