Genome-wide identification of laccase gene family in three Phytophthora species

Abstract

Phytophthora spp. is a primary pathogen in oomycete, causing economically and environmentally devastating epidemics of plants. Laccases have been found in all domains of life but have not been reported in oomycte. In this paper, laccase genes of Phytophthora spp. were identified in three genomes (Phytophthora capsici, Phytophthora sojae and Phytophthora ramorum). 18 laccase genes were identified in total, including four in P. capsici genome, six in P. sojae genome and eight in P. ramorum genome. Most of the predicted gene models shared typical fungal laccase character, possessing three conserved positions with one cysteine and ten histidine residues at these positions. Phylogenetic analysis illustrated that laccases from Phytophthora clustered into four clades, while fungal laccases clustered together. The results provided the theoretical ground for new hypotheses about the roles laccases in oomycetes and may guide the future research of these enzymes.

The contrasting roles of aquatic fungi and oomycetes in the degradation and transformation of polymeric organic matter

“…In contrast, all 18 laccase genes and expansion of effector protein families including pectinases are present in plant pathogenic oomycetes such as Phytophthora sp. (Feng and Li , 2014; Feng et al ; McGowan and Fitzpatrick ). This may hint to a sharp dichotomy between mostly terrestrial plant pathogens and freshwater saprophytic oomycetes such as Saprolegnia sp., Achlya sp., and Leptolegnia sp.…”

Phylogenetic and Functional Diversity of Saprolegniales and Fungi Isolated from Temperate Lakes in Northeast Germany

“…Laccases significantly contribute to the pathogenicity and defense mechanisms of phytopathogenic fungi [47]. Also, laccase genes have been identified in four terrestrial phytopathogenic oomycetes species [48][49][50][51], confirming the importance of laccases for their pathogenicity. This enzyme, for example, is responsible for the pathogenicity of Plasmopara viticola in grapevine [52].…”

Novel Fungicide 4-Chlorocinnamaldehyde Thiosemicarbazide (PMDD) Inhibits Laccase and Controls the Causal Agent of Take-All Disease in Wheat, Gaeumannomyces graminis var. tritici

“…Laccase is absent in oomycetes and replaced by a multi-copper oxidase analogue. 43 There are substantial differences in the structure between laccase and multi-copper oxidase, 44 which may be the key to the insensitivity of oomycetes to PMDD. PMDD exhibits a much better protective fungicidal activity than curative activity (Table 1), which implies that PMDD should only be applied before disease outbreak.…”

“…This may mean that a higher number of laccases may compensate for PMDD targeting, because it could lead to greater chance of incompatibility with PMDD. Laccase is absent in oomycetes and replaced by a multi-copper oxidase analogue . There are substantial differences in the structure between laccase and multi-copper oxidase, which may be the key to the insensitivity of oomycetes to PMDD.…”