Protein disulfide isomerase like 5-1 is a susceptibility factor to plant viruses

Ping Yang, Thomas Lüpken, Antje Habekuss, Goetz Hensel, Burkhard Steuernagel, Benjamin Kilian, Ruvini Ariyadasa, Axel Himmelbach, Jochen Kumlehn, Uwe Scholz, Frank Ordon, Nils Stein

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

Protein disulfide isomerases (PDIs) catalyze the correct folding of proteins and prevent the aggregation of unfolded or partially folded precursors. Whereas suppression of members of the PDI gene family can delay replication of several human and animal viruses (e.g., HIV), their role in interactions with plant viruses is largely unknown. Here, using a positional cloning strategy we identified variants of PROTEIN DISULFIDE ISOMERASE LIKE 5-1 (HvPDIL5-1) as the cause of naturally occurring resistance to multiple strains of Bymoviruses. The role of wild-type HvPDIL5-1 in conferring susceptibility was confirmed by targeting induced local lesions in genomes for induced mutant alleles, transgene-induced complementation, and allelism tests using different natural resistance alleles. The geographical distribution of natural genetic variants of HvPDIL5-1 revealed the origin of resistance conferring alleles in domesticated barley in Eastern Asia. Higher sequence diversity was correlated with areas with increased pathogen diversity suggesting adaptive selection for bymovirus resistance. HvPDIL5-1 homologs are highly conserved across species of the plant and animal kingdoms implying that orthologs of HvPDIL5-1 or other closely related members of the PDI gene family may be potential susceptibility factors to viruses in other eukaryotic species.

Original languageEnglish
Pages (from-to)2104-2109
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume111
Issue number6
DOIs
Publication statusPublished - 11 Feb 2014
Externally publishedYes

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