Allister Crow

@allistercrow.bsky.social

Structural Microbiologist

And now published as an Observation! Many congrats to @weeboont.bsky.social for discovering that AsmA superfamily proteins, YhdP/TamB/YdbH, localize to the cell poles in E. coli, curiously AFTER division has occurred! 1/3 #MicroSky journals.asm.org/doi/10.1128/...

Polar localization of putative phospholipid transporters in Escherichia coli | mBio

The outer membrane (OM) of Gram-negative bacteria serves as an effective permeability barrier and confers intrinsic antibiotic resistance. This barrier function requires distinct distribution of lipid...

journals.asm.org

Shu-Sin Chng@figlegend.bsky.social · last yr.

@weeboont.bsky.social talked about our lab's recent preprint where we report AsmA superfamily proteins, believed to be phospholipid transporters, localizing to cell poles in E. coli. Really interesting observations, with impt implications for OM assembly! Read it 👇! www.biorxiv.org/content/10.1...

So happy to announce our new preprint, “A geothermal amoeba sets a new upper temperature limit for eukaryotes.” We cultured a novel amoeba from Lassen Volcanic NP (CA, USA) that divides at 63°C (145°F) 🔥 - a new record for euk growth! #protistsonsky 🧵

bioRxiv Microbiology@biorxiv-microbiol.bsky.social · 8mo ago

A geothermal amoeba sets a new upper temperature limit for eukaryotes https://www.biorxiv.org/content/10.1101/2025.11.24.690213v1

(BioRxiv All) Paenitracins, a novel family of bacitracin-type nonribosomal peptide antibiotics produced by plant-associated Paenibacillus species: The growing threat of antimicrobial resistance necessitates the discovery of novel antibiotics with activity against… #BioRxiv #MassSpecRSS

Paenitracins, a novel family of bacitracin-type nonribosomal peptide antibiotics produced by plant-associated Paenibacillus species

The growing threat of antimicrobial resistance necessitates the discovery of novel antibiotics with activity against drug-resistant pathogens. Members of the genus Paenibacillus are a rich source of nonribosomal peptides (NRPs), including well-known antibiotics such as polymyxins, paenibacterin and tridecaptins. Here we use a targeted Mass-QL-based mass spectrometry approach to identify the NRPs produced by a collection of 227 taxonomically diverse plant-associated Paenibacillus strains, providing detailed insights into their NRP-producing potential. Using MassQL to zoom in specifically on NRPs containing basic amino acids, we discovered a novel family of bacitracins, which we designated paenitracins. The paenitracins are the first bacitracin-type peptides reported in Paenibacillus, and are distinguished from canonical bacitracins by three previously unseen amino acid substitutions. The paenitracins exhibit potent activity against Gram-positive pathogens, including vancomycin-resistant Enterococcus faecium E155. Our work provides a novel metabolomics- and genomics-guided workflow for the discovery of bioactive NRPs as a strategy to prioritize natural product chemical space and accelerate antibiotic discovery.

dlvr.it

The outer membrane of Gram-negative bacteria blocks many antibiotics. Our latest work reveals that L-type pyocins bypass this barrier by inactivating the BAM complex, killing Pseudomonas aeruginosa without entering the cell, providing a new blueprint for beating antibiotic resistance.

A Protein Antibiotic Inhibits the BAM Complex to Kill Without Cell Entry

Many antibiotics are ineffective against Gram-negative pathogens such as Pseudomonas aeruginosa because they cannot penetrate the bacterial outer membrane. Here, we show that protein antibiotics calle...

biorxiv.org

Why make a cofactor when you can get it for free? Our work, led by @fabianmunder.bsky.social, shows that bacteria from 22 phyla use the high-affinity transporter PqqU to obtain the redox cofactor PQQ from the environment as an alternative to cofactor synthesis. www.science.org/doi/10.1126/...

High-affinity PQQ import is widespread in Gram-negative bacteria

Diverse bacteria use the high-affinity membrane transport protein PqqU to scavenge the nutrient PQQ from the environment.

science.org