Zhiteng Chen, Jingqun

Ao, Wenchuan Yang, Liping Jiao, Tianling Zheng, Xinhua Chen,Appl

Microbiol Biotechnol, 2013. 97:10381-10390

A fungal strain,Penicillium chrysogenumA096,was isolated from an Arctic sediment

sample. Its culture supernatant inhibited mycelial growth of some plant

pathogenicfungi. After saturation ofP.

chrysogenumA096 culture supernatant with ammonium sulfate and ion exchange

chromatography, a novel antifungal protein (Pc-Arctin) was purified

andidentified by matrix assisted laser desorption ionization-time offlight-time

of flight-mass spectrometry (MALDI-TOF-TOF-MS). The gene encoding for Pc-Arctin

consisting of 195 nucleotides was cloned from P. chrysogenum A096 to confirm

themass spectrometry result. Pc-Arctin displays antifungal activityagainstPaecilomyces variotii,Alternaria longipes, andTrichoderma virideat minimum inhibitory

concentrations(MIC) of 24, 48, and 192 ng/disc, respectively. Pc-Arctin wasmost

sensitive to proteinase K and then to trypsin but insensitive to papain.

Pc-Arctin possesses high thermostability andcannot be antagonized by common

surfactants, except forsodium dodecyl sulfate (SDS). Divalent ions, such as Mn²⁺,Mg²⁺,

and Zn²⁺, inhibited the antifungal activity of

Pc-Arctin.Hemagglutination assays showed that Pc-Arctin had nohemagglutinating

or hemolytic activity against red blood cells(RBC) from rabbits, rats, and

guinea pigs. Therefore, Pc-Arctinfrom ArcticP. chrysogenummay represent a novel antifungalprotein with

potential for application in controlling plant pathogenic fungal infection.

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