Kumaran Ramamurthi

@ramamurthilab.bsky.social

Scientist studying protein localization in bacteria. We also design artificial bacteria to deliver chemotherapeutics to #cancer cells. All views are my own. https://scholar.google.com/citations?user=t9UM04YAAAAJ&hl=en

Another chapter of my thesis is out! We asked whether we could pair proteome-wide AlphaFold screening with Tn-seq to identify biologically relevant protein-protein interactions. We identify ClcR (formerly YerH) as a component of the Rod complex in Gram-positive bacteria. www.pnas.org/doi/10.1073/...

A broadly conserved gram-positive lipoprotein regulates cell elongation | PNAS

The cell wall peptidoglycan (PG) protects virtually all bacteria from osmotic lysis and specifies cell shape. Synthesis of this exoskeleton is carr...

pnas.org

We've been learning a lot about how Enterococcus faecalis interacts with neutrophils lately. In our latest preprint, @harisantypas.bsky.social describes how lactic acid from E. faecalis dampens neutrophil metabolism leading to NETosis and phagoytosis suppression. #microsky

bioRxiv Microbiology@biorxiv-microbiol.bsky.social · 2mo ago

Enterococcus faecalis biofilm rewires neutrophil metabolism to suppress antimicrobial functions https://www.biorxiv.org/content/10.64898/2026.06.18.733107v1

This study further highlights the power of integrating advanced cryo-EM with computational structural biology to assign functions to the vast repertoire of proteins encoded within microbial “dark matter,” where conventional annotation approaches often fall short.

Taylor Updegrove presenting his work at #ASMicrobe. His "coming soon" paper proposes that a subpopulation of early-sporulating B. subtilis cells signals to other cells to initiate biofilm formation via secreted glycerol (normally an intracellular metabolite) that acts as a extracellular "morphogen"

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@felixrl.bsky.social presenting his work at #ASMicrobe today. His preprint follows up on his recent work on orthogonal cell division in S. aureus and reports that PcdA, the division septum placement factor, is required for forming staphylococcal abscess colonies.

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Kumaran Ramamurthi@ramamurthilab.bsky.social · 5mo ago

@felixrl.bsky.social reported that PcdA mediates orthogonal cell division in #Staphylococcus aureus: www.nature.com/articles/s41.... But what’s the point? Well, forming staphylococcal abscess communities to evade host immune responses requires this mode of division: www.biorxiv.org/cgi/content/...

@vanipande.bsky.social presenting her work at #ASMicrobe today.... Check out her recent preprint about a spontaneously inserting integral membrane protein that localized by recognizing a lipid cue

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Kumaran Ramamurthi@ramamurthilab.bsky.social · 2mo ago

Bacterial transmembrane proteins usually localize inside the cell by "finding" a pre-localized protein, but how did the 1st protein get there? @vanipande.bsky.social found a protein in #B.subtilis that localizes by recognizing a *lipid* localization cue. #Microsky www.biorxiv.org/content/10.6...

Tonight we continue our gram-negative cocci series 🎙️ This time we’re talking about the background singers of the group: non-pathogenic Neisseria + Neisseria and Moraxella species that break the gram-negative cocci rule. 7 PM

@biorxiv-microbiol.bsky.social Who knew ParB-CTPase fold can kill!!! A protein fold best known for segregating chromosomes…can be transformed into a potent antibacterial toxin in some plant and animal pathogens. www.biorxiv.org/content/10.6...

Repurposing a chromosome segregation ParB-CTPase fold into an ATPase toxin for contact-dependent growth inhibition in plant and animal pathogens

Bacterial competition drives the evolution of antibacterial mechanisms, yet how new activities arise remains poorly understood. A major route to innovation is the reuse of pre-existing genetic systems, whereby conserved protein modules are repurposed in new biological contexts to generate new capabilities. Here, we show that the ParB-CTPase fold, a conserved nucleotide-binding module best known for its role in chromosome segregation, can be functionally repurposed as an antibacterial toxin. We identify ToxB, a ParB-like domain embedded within the polymorphic toxin region of contact-dependent inhibition systems and show that it functions as a potent antibacterial effector. Structural and biochemical analyses reveal that ToxB retains the core architecture of the ParB-CTPase fold but lacks DNA-binding capability and preferentially binds ATP. This shift in nucleotide specificity underpins a distinct mode of action, in which ATP binding and hydrolysis trigger rapid nucleoid compaction, chromosome segregation defects, oxidative stress, cell chaining, and ultimately cell lysis. ToxB also exhibits toxic activity in plant cells, suggesting that it targets conserved cellular processes. Together, these findings provide direct experimental evidence that the ParB-NTPase fold is biologically versatile and can be repurposed for biological roles fundamentally distinct from its ancestral function in DNA segregation. ### Competing Interest Statement The authors have declared no competing interest. Wellcome Trust, https://ror.org/029chgv08, 221776/Z/2/Z, 227755/Z/23/Z Biotechnology and Biological Sciences Research Council, https://ror.org/00cwqg982, BB/X01097X/1 Diamond Light Source, MX32728

biorxiv.org