(not) Imran Khan
@imrsankhan.bsky.social
140 followers 220 following 16 posts
UCC. Staph man. Insane for the membrane. He/Him.
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imrsankhan.bsky.social
Our work deciphering the substrate preferences of a di-/tripeptide transporter from S. aureus is now available as a proof at @plos.org Pathogens! Big thanks to the reviewers and to all the brilliant co-authors, particularly Callum who helped get those last few crucial experiments across the line
Defined roles for the Staphylococcus aureus POT transporter DtpT in di/tripeptide uptake and glutathione utilisation inside human macrophages
Author summary The environments where bacterial pathogens thrive are often rich in proteins and their degradation products, including oligopeptides, which can be taken up by the bacterium and used as ...
journals.plos.org
Reposted by (not) Imran Khan
jasonyanglab.org
Very happy to share some more good news. Our collaboration with Jeffrey Boyd's lab is now published at J Inorganic Biochemistry! Here, Jeff found that iron limitation reprograms S. aureus metabolism towards fermentation. We're grateful to be part of this study.

www.sciencedirect.com/science/arti...
Fermentative growth decreases the iron demand of Staphylococcus aureus
Iron (Fe) is an essential nutrient for S. aureus survivability and pathogenesis, but excess Fe can catalyze the formation of toxic oxygen radicals, em…
www.sciencedirect.com
imrsankhan.bsky.social
Our work deciphering the substrate preferences of a di-/tripeptide transporter from S. aureus is now available as a proof at @plos.org Pathogens! Big thanks to the reviewers and to all the brilliant co-authors, particularly Callum who helped get those last few crucial experiments across the line
Defined roles for the Staphylococcus aureus POT transporter DtpT in di/tripeptide uptake and glutathione utilisation inside human macrophages
Author summary The environments where bacterial pathogens thrive are often rich in proteins and their degradation products, including oligopeptides, which can be taken up by the bacterium and used as ...
journals.plos.org
imrsankhan.bsky.social
Cheers Emm!! Very glad to finally see this out in the world
Reposted by (not) Imran Khan
Reposted by (not) Imran Khan
chrismulligan.bsky.social
Really pleased to share some recent work from our lab now published in Comms Bio. Here, we’ve identified and characterised a peculiar TRAP transporter binding protein from B. pertussis that we think uses a membrane component from a completely different transporter family.
rdcu.be/eAr8v
A new class of binding-protein dependent solute transporter exemplified by the TAXI-GltS system from Bordetella pertussis
Communications Biology - Identification and characterization of an unusual tri-domain TRAP transporter binding protein from Bordetella pertussis reveals insight into the diversity of binding...
rdcu.be
imrsankhan.bsky.social
Very important new paper regarding amino acid acquisition inside staph-infected macrophages! Key role for BCAAs + nice evidence that host cell nutrients can be conveyed to bacteria in the phagosome to facilitate growth... Big implications for host-path interactions. Great work!
Inactivation of branched-chain amino acid uptake halts Staphylococcus aureus growth and induces bacterial quiescence within macrophages
Author summary Staphylococcus aureus is a prominent human pathogen causing acute and chronic disease. It is facultatively intracellular and can reside within many host cell types, including profession...
journals.plos.org
Reposted by (not) Imran Khan
biorxiv-microbiol.bsky.social
A single transcriptional regulator is crucial for the adaptation of Staphylococcus aureus to diverse niches https://www.biorxiv.org/content/10.1101/2025.08.01.668060v1
Reposted by (not) Imran Khan
biorxivpreprint.bsky.social
Commensal to pathogen switch in Streptococcus pneumoniae is governed by a thermosensing master regulator https://www.biorxiv.org/content/10.1101/2025.05.23.655729v1
Reposted by (not) Imran Khan
biorxiv-microbiol.bsky.social
Competition with Pseudomonas aeruginosa induces Staphylococcus aureus in an antibiotic-tolerant viable but non culturable state https://www.biorxiv.org/content/10.1101/2025.04.30.651255v1
Reposted by (not) Imran Khan
Reposted by (not) Imran Khan
ttsukaza.bsky.social
Just posted on bioRxiv!

We reveal the structure of the MurJ/LysM (JM) complex.
A small phage protein, LysM (37 residues), binds to MurJ like a wedge and freezes its motion.

www.biorxiv.org/content/10.1...