Skip to main content
ARS Home » Plains Area » Fargo, North Dakota » Edward T. Schafer Agricultural Research Center » Cereal Crops Research » Research » Publications at this Location » Publication #401965
Research Project: Host-Pathogen Interactions Affecting Wheat and Barley

Location: Cereal Crops Research

Title: The contribution of extracellular protease to virulence and virulence-associated behaviors of Xanthomonas translucens pv. translucens

Author
item ALAOFIN, SEFUNMI - North Dakota State University
item Schachterle, Jeffrey

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 2/27/2023
Publication Date: 3/2/2023
Citation: Alaofin, S., Schachterle, J.K. 2023. The contribution of extracellular protease to virulence and virulence-associated behaviors of Xanthomonas translucens pv. translucens. Meeting Abstract. 2:12.

Interpretive Summary:

Technical Abstract: Xanthomonas translucens pv. translucens (Xtt) is the causative agent of bacterial leaf streak in barley leading to up to 40% yield loss. Xanthomonas translucens strains are grouped by pathovar based on host range, however advances in genome sequencing are uncovering new evidence that each pathovar encompass large amounts of genetic diversity. We have found variation in extracellular enzymatic protease activity in Xtt isolates with a complete absence of extracellular protease activity in the North Dakota isolate ‘Barley B1’. By probing into the genome of Xtt isolates using publicly available genome sequences, we found this protease to be well conserved in Xtt generally except for ‘Barley B1’ in which a 16 amino acid deletion was found. Because of the sequence variation between Barley B1 and other Xtt strains in the gene encoding extracellular protease along with the phenotypic differences, this research aims to functionally evaluate and characterize the contribution of extracellular protease to virulence and virulence-associated behaviors of Xtt. Genomic DNA (gDNA) was isolated from different Xtt isolates and the protease gene was amplified from the isolated gDNA and cloned into plasmid pBBR1MCS-5 using an in-vivo assembly approach. Plasmids containing cloned protease from various Xtt isolates were recovered from transformed E. coli, purified, and used to transform ‘Barley B1’. The transformed Barley B1 was then assessed for complementation of protease activity and further phenotypic characterization.