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Difference between revisions of "User:Kim Orth"
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| − | + | Kim Orth is a Professor of Molecular Biology and Biochemistry and is an Investigator for the Howard Hughes Medical Institute. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science. | |
| − | + | The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms. | |
| − | + | The marine bacterium Vibrio parahaemolyticus is the worldwide leading cause of seafood-borne acute gastroenteritis. The Orth Lab is working on the two V. parahaemolyticus type 3 secretion systems (T3SS1 and T3SS2) and their bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by these bacterial pathogens. For decades, this pathogen has been studied exclusively as an extracellular bacterium. However, recent studies from our lab have revealed the pathogen’s ability to invade and replicate within host cells using the second T3SS2. New host mechanisms that are exploited by this bacterium to survive and escape. Work in the Orth Lab at UT Southwestern is accomplished using a broad range of tools, including biochemistry, molecular microbiology, protein chemistry, structural biology, yeast genetics, cell biology, biophysics and more. | |
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| − | '' | + | The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase <cite>Peng2024</cite>. AvrB contains a domain or fold called Fido <cite>Kinch2009</cite>. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells <cite>Peng2024</cite>. '''AvrB is the founding member of glycosyltransferases with Fido fold''', belonging to family of [[GT138]]. |
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| + | Kim contributed to studies on: | ||
| + | * [[GT138]] ''Pseudomonas syringae'' rhamnosyltransferase '''AvrB''' <cite>Peng2024</cite> | ||
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| − | # | + | #Peng2024 pmid=38354245 |
| + | #Kinch2009 pmid=19503829 | ||
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| − | [[Category:Contributors| | + | [[Category:Contributors|Peng,Wei]] |
Revision as of 11:39, 8 December 2025
Kim Orth is a Professor of Molecular Biology and Biochemistry and is an Investigator for the Howard Hughes Medical Institute. She is a W. W. Caruth, Jr. Scholar in Biomedical Research and holds the Earl A. Forsythe Chair in Biomedical Science.
The Orth Lab is interested in elucidation the activity of virulence factors from pathogenic bacteria so that we can gain novel molecular insight into eukaryotic signaling systems. They have discovered novel chemistry, including Ser/Thr acetylation and AMPylation, used by bacterial virulence factors to manipulate the host cell signaling. In some cases, they found the eukaryotic host also uses these novel mechanisms.
The marine bacterium Vibrio parahaemolyticus is the worldwide leading cause of seafood-borne acute gastroenteritis. The Orth Lab is working on the two V. parahaemolyticus type 3 secretion systems (T3SS1 and T3SS2) and their bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by these bacterial pathogens. For decades, this pathogen has been studied exclusively as an extracellular bacterium. However, recent studies from our lab have revealed the pathogen’s ability to invade and replicate within host cells using the second T3SS2. New host mechanisms that are exploited by this bacterium to survive and escape. Work in the Orth Lab at UT Southwestern is accomplished using a broad range of tools, including biochemistry, molecular microbiology, protein chemistry, structural biology, yeast genetics, cell biology, biophysics and more.
The Orth lab discovered that the bacterial effector protein AvrB is an unprecedented glycosyltransferase [1]. AvrB contains a domain or fold called Fido [2]. AvrB catalyzes the transfer of rhamnose from UDP-rhamnose to a threonine residue of its protein substrate in host cells [1]. AvrB is the founding member of glycosyltransferases with Fido fold, belonging to family of GT138.
Kim contributed to studies on:
- Peng W, Garcia N, Servage KA, Kohler JJ, Ready JM, Tomchick DR, Fernandez J, and Orth K. (2024). Pseudomonas effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4. Sci Adv. 2024;10(7):eadd5108. DOI:10.1126/sciadv.add5108 |
- Kinch LN, Yarbrough ML, Orth K, and Grishin NV. (2009). Fido, a novel AMPylation domain common to fic, doc, and AvrB. PLoS One. 2009;4(6):e5818. DOI:10.1371/journal.pone.0005818 |