Fungal proteinase expression in the interaction of the plant pathogen Magnaporthe poae with its host.
Infection by pathogenic fungi involves breaching the outer layer of the host by either mechanical or enzymatic means. Subtilisin-like proteinases are considered to be important in the infection process of entomopathogenic, nematophagous, and mycoparasitic fungi. Little is known regarding the expression of such proteinases by plant pathogenic fungi. Magnaporthe poae, a fungal pathogen of Kentucky bluegrass, expressed a subtilisin-like proteinase, proteinase Mp1, in the infected roots. Antibody was produced against the purified enzyme. From immunoblot analysis, expression of the proteinase in infected roots correlated with increasing severity of disease symptoms. Sequence analysis of a genomic clone indicated proteinase Mp1 was homologous to other fungal subtilisin-like proteinases. DNA gel blot analysis indicated proteinase Mp1 was encoded by a small gene family.
Department of Plant Pathology, Rutgers University, New Brunswick, NJ 08903, USA.
L
L
Sreedhar
D Y
DY
Kobayashi
T E
TE
Bunting
B I
BI
Hillman
F C
FC
Belanger
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D016681:Genome, Fungal; D020082:Magnaporthe / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D005810:Multigene Family / Q000235:genetics; D010935:Plant Diseases / Q000382:microbiology; D018517:Plant Roots / Q000378:metabolism / Q000382:microbiology; D006109:Poaceae / Q000382:microbiology*; D017386:Sequence Homology, Amino Acid; D013381:Subtilisins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D005656:Fungal Proteins; D010450:Endopeptidases; D013381:Subtilisins