About

Celia W. Goulding is a Chair and Professor in the Department of Molecular Biology and Biochemistry at UC Irvine, with additional appointments in the School of Pharmacy & Pharmaceutical Sciences. She holds a B.S. in Chemistry & Mathematics and a Ph.D. in Physical Organic Chemistry from Kings College, London, UK. Her postdoctoral research was conducted at the University of Michigan in Biochemistry, and she has held research faculty positions at UCLA in TB Structural Genomics. Her research focuses on utilizing proteomic and crystallographic techniques to elucidate and characterize new systems of protein complexes in Mycobacterium tuberculosis. Her laboratory aims to shift the focus of structural biology from individual proteins to molecular assemblies, particularly those containing potential anti-TB drug targets and membrane components. Key areas of investigation include the structural and biochemical dissection of mycobacterial heme uptake systems, contact-dependent growth inhibition mechanisms in gram-negative bacteria, and the structural basis of bacterial toxin and immunity protein complexes. Her work has contributed to understanding heme degradation by M. tuberculosis enzymes, the structural diversity of bacterial contact-dependent growth inhibition effectors, and the molecular mechanisms underlying bacterial iron acquisition and toxin activation. Goulding's research has advanced knowledge in bacterial pathogenesis, protein complex structures, and potential therapeutic targets for tuberculosis.

Research topics

• Biology
• Biochemistry
• Microbiology
• Computational biology
• Cell biology
• Genetics
• Bioinformatics

Selected publications

• Bacteria deliver a microtubule-binding protein into mammalian cells to promote colonization

  Science · 2026-02-19 · 2 citations

  article

  Pathogenic Bordetella bacteria use protein adhesins to infect the ciliated respiratory epithelia of vertebrate hosts. In this work, we show that the filamentous hemagglutinin FhaB adhesin of Bordetella carries a C-terminal microtubule-binding domain (FhaB-CT), which is translocated into host cells to promote colonization. FhaB-CT delivery is required to occupy a niche at the base of cilia in airway epithelia, and mutant bacteria lacking this domain are defective for nasal colonization. These observations suggest that FhaB-CT is transferred into motile respiratory cilia to interact with core axonemal microtubules. We propose that Bordetella adheres initially to the tips of cilia and then deploys multiple FhaB adhesins to migrate to the base of the cilia forest, where the bacteria resist removal by the mucociliary “escalator” that normally clears the respiratory tract of microbes.

  PublisherDOI

• MassIVE MSV000100589 - A non-canonical histidine kinase (Rv1127c, VadK) from Mycobacterium tuberculosis.

  2026-01-01

  datasetOpen access1st authorCorresponding
  OA PDFDOI

• MassIVE MSV000101031 - Phosphorylation of Mycobacterium tuberculosis VadK (RV1127c) data

  2026-01-01

  datasetOpen access1st authorCorresponding
  OA PDFDOI

• MassIVE MSV000100985 - Phosphorylation data for a non-canonical histidine kinase (Rv1127c, VadK) from Mycobacterium tuberculosis.

  California Digital Library · 2026-01-01

  datasetOpen access1st authorCorresponding
  OA PDFDOI

• MassIVE MSV000100587 - A non-canonical histidine kinase (Rv1127c, VadK) from Mycobacterium tuberculosis.

  2026-01-01

  datasetOpen access1st authorCorresponding
  OA PDFDOI

• Elongation Factor Tu Acts as a Chaperone to Activate an Antibacterial <scp>RNase</scp> Toxin

  Molecular Microbiology · 2026-01-20 · 2 citations

  articleOpen access

  ABSTRACT Many Gram‐negative bacterial species use contact‐dependent growth inhibition (CDI) systems to deliver toxic proteins into neighboring competitors. CDI + strains deploy CdiA effector proteins, which translocate their C‐terminal toxin (CT) domains into target bacteria through a receptor‐mediated delivery pathway. To protect against auto‐intoxication, CDI + bacteria also produce CdiI immunity proteins that neutralize CT toxin activity. Here, we present the crystal structure of the CT·CdiI O32:H37 complex from Escherichia coli O32:H37. CT O32:H37 adopts the same fold as the tRNase domain of colicin D, and the nucleases share similar catalytic centers. However, unlike colicin D, which cleaves the anticodon loops of tRNA Arg isoacceptors, CT O32:H37 exhibits nonspecific RNase activity. Notably, we find that endogenous elongation factor Tu (EF‐Tu) co‐purifies with the over‐produced CT·CdiI O32:H37 complex. Although EF‐Tu does not bind stably to CT O32:H37 in the absence of CdiI O32:H37 , the translation factor is required for toxic RNase activity in vitro. AlphaFold 3 modeling and site‐directed mutagenesis indicate that CT O32:H37 interacts with the N‐terminal GTPase domain of EF‐Tu. EF‐Tu appears to stabilize residue Trp52 within the hydrophobic core of the toxin, which in turn supports the RNase active site through an unusual hydrogen‐bonding interaction with the catalytic His67 residue. Thus, EF‐Tu is hijacked as an essential co‐factor to organize the toxin's catalytic center.

  PublisherOA PDFDOI

• MassIVE MSV000100591 - A non-canonical histidine kinase (Rv1127c, VadK) from Mycobacterium tuberculosis.

  2026-01-01

  datasetOpen access1st authorCorresponding
  OA PDFDOI

• Redox regulated auto-processing controls delivery of an antibacterial cysteine peptidase toxin

  bioRxiv (Cold Spring Harbor Laboratory) · 2026-05-08

  articleOpen accessSenior author

  Abstract Contact-dependent growth inhibition (CDI) is a mechanism of inter-bacterial competition mediated by CdiA effectors, which deliver polymorphic C-terminal toxins (CT) into neighboring competitors. StbD from Citrobacter rodentium DBS100 is an unusual CdiA-like protein that carries a C-terminal cysteine peptidase toxin. Crystallography reveals that StbD-CT is composed of an N-terminal cytoplasm-entry domain connected to a C39 family peptidase by a flexible linker. The entry domain hijacks membrane-embedded YajC for translocation into the target-cell cytosol where the peptidase inactivates type II topoisomerases. Intoxication leads to a loss of DNA super-helicity, impaired chromosome segregation and cell filamentation. In addition to cleaving topoisomerases, StbD-CT exhibits auto-proteolytic processing under reducing conditions, and this activity is required for target cell intoxication. We propose that StbD-CT remains tethered to the cell periphery via interactions with YajC after delivery. Auto-processing releases the peptidase, enabling the domain to penetrate into the cell interior where it cleaves nucleoid-associated topoisomerases. Together, these findings identify a proteolytic effector that deactivates type II topoisomerases and reveal a redox regulatory strategy that coordinates toxin activation with intercellular delivery.

  PublisherOA PDFDOI

• A periplasmic protein complex mediates arabinofuranosyltransferase activity and intrinsic drug resistance in <i>Mycobacterium tuberculosis</i>

  Science Advances · 2026-04-01

  articleOpen access

  (Mtb) is a major barrier to effective tuberculosis (TB) treatment and is largely due to its complex, impermeable cell envelope. We identified a periplasmic protein complex comprising FecB and Rv3035 that is essential for maintaining envelope integrity and mediating intrinsic multidrug resistance in Mtb. FecB interacts with Rv3035, forming a stable heterodimer that associates with the cell envelope biosynthesis protein AftB. We report the structures of Rv3035 alone and in complex with FecB and identify critical residues for complex formation and function. Coessentiality and genetic interaction analyses support a functional link between FecB, Rv3035, and AftB, an arabinofuranosyltransferase that synthesizes arabinogalactan and lipoarabinomannan. Loss of FecB or Rv3035 disrupted AftB-mediated arabinan synthesis, suggesting that these proteins support AftB's enzymatic activity. FecB is required for Mtb virulence in mice, underscoring its physiological relevance. These findings highlight FecB, Rv3035, and AftB as promising therapeutic targets.

  PublisherDOI

• MassIVE MSV000100588 - A non-canonical histidine kinase (Rv1127c, VadK) from Mycobacterium tuberculosis.

  2026-01-01

  datasetOpen access1st authorCorresponding
  OA PDFDOI

Recent grants

• Molecular mechanisms of antibacterial CDI toxin activation

  NIH · $1.2M · 2016–2021

• Structure-function analysis of polymorphic CDI toxin-immunity protein complexes a

  NIH · $1.7M · 2012–2017

• T32 for Training in Microbiology & Infectious Diseases

  NIH · $738k · 2019–2030

• Project 3 - The Critical Role of Membrane Transport

  NIH · $39.7M · 2012–2024

• NIH Grant R01AI081161

  NIH · $1.8M · 2015

Frequent coauthors

• David Eisenberg

  Howard Hughes Medical Institute

  32 shared

• William R. Jacobs

  Albert Einstein College of Medicine

  21 shared

• Nicholas Chim

  19 shared

• Suzanne M. Hingley‐Wilson

  University of Surrey

  18 shared

• Christopher S. Hayes

  University of California, Santa Barbara

  18 shared

• Carolyn B. Marks

  University of Southern California

  16 shared

• Annie Z. Dai

  16 shared

• Robert G. Russell

  16 shared

Labs

• Goulding LabPI

Education

• B.S., Chemistry & Mathematics

  Kings College, London, UK

• Ph.D., Physical Organic Chemistry

  Kings College, London, UK