Allison Zhao
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Allison Zhao has a total of 12 co-authors. Here are the top co-authors by number of shared publications:
Acacia F. Dishman
Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226, USA
1 shared publication- Angela Ballesteros
Section on Sensory Physiology and Biophysics, National Institute on Deafness and Other Communication Disorders
1 shared publication - Brian F. Volkman
Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, USA
1 shared publication - David N. Garboczi
Structural Biology Section, Research Technologies Branch, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
1 shared publication - Ernest Y. Lee
Department of Bioengineering, Department of Chemistry & Biochemistry, and California, NanoSystems Institute, University of California, Los Angeles, CA, USA
1 shared publication - Gerard C. L. Wong
Department of Bioengineering, University of California Los Angeles
1 shared publication
Latest Publications
- Open Access
- 6 June 2025
- Published by American Association for the Advancement of Science (AAAS) in Science Advances
- Vol. 11 (23) , eads2675
Chemokines kill bacteria without triggering antimicrobial resistance by binding anionic phospholipids
Classically, chemokines coordinate leukocyte trafficking; however, many chemokines also have direct antibacterial activity. The bacterial killing mechanism of chemokines and the biochemical properties that define which members of the chemokine superfamily are antimicrobial remain poorly understood. We report that the antimicrobial activity of chemokines is defined by their ability to bind phosphatidylglycerol and cardiolipin, two anionic phospholipids commonly found in the bacterial plasma membrane. We show that only chemokines able to bind these two phospholipids kill bacteria and that they exert rapid bacteriostatic and bactericidal effects with a higher potency than the antimicrobial peptide β-defensin 3. Both biochemical and genetic interference with the chemokine-cardiolipin interaction impaired microbial growth arrest, bacterial killing, and membrane disruption by chemokines. Moreover, unlike conventional antibiotics, Escherichia coli failed to develop resistance when placed under increasing antimicrobial chemokine pressure in vitro. Thus, we have identified cardiolipin and phosphatidylglycerol as binding partners for chemokines responsible for chemokine antimicrobial action.
- 6 June 2025
- Published by American Association for the Advancement of Science (AAAS) in Science Advances
- Vol. 11 (23) , eads2675
Open AccessChemokines kill bacteria without triggering antimicrobial resistance by binding anionic phospholipids
Classically, chemokines coordinate leukocyte trafficking; however, many chemokines also have direct antibacterial activity. The bacterial killing mechanism of chemokines and the biochemical properties that define which members of the chemokine superfamily are antimicrobial remain poorly understood. We report that the antimicrobial activity of chemokines is defined by their ability to bind phosphatidylglycerol and cardiolipin, two anionic phospholipids commonly found in the bacterial plasma membrane. We show that only chemokines able to bind these two phospholipids kill bacteria and that they exert rapid bacteriostatic and bactericidal effects with a higher potency than the antimicrobial peptide β-defensin 3. Both biochemical and genetic interference with the chemokine-cardiolipin interaction impaired microbial growth arrest, bacterial killing, and membrane disruption by chemokines. Moreover, unlike conventional antibiotics, Escherichia coli failed to develop resistance when placed under increasing antimicrobial chemokine pressure in vitro. Thus, we have identified cardiolipin and phosphatidylglycerol as binding partners for chemokines responsible for chemokine antimicrobial action.