Metarhizium anisopliae host–pathogen interaction: differential immunoproteomics reveals proteins involved in the infection process of arthropods

Santi, Lucélia; Silva, Walter O.B.; Pinto, Antônio Frederico Michel; Schrank, Augusto; Vainstein, Marilene Henning

doi:10.1016/j.funbio.2010.01.006

Cited by 45 publications

(43 citation statements)

References 49 publications

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“…The proteins recognized in vitro by antibodies in this work probably have the same antigenic determinants that induce antibodies in vivo. This approach has frequently been used to identify immunogenic proteins and, consequently, new targets to diagnose several diseases [41][42][43][44][45][46][47][48][49][50][51][52][53][54]. Although similar results have been achieved in cryptococcosis using murine [55] and koala models [56], this is the first report in human beings.…”

Section: Discussionmentioning

confidence: 85%

Immunoproteomics and Immunoinformatics Analysis of Cryptococcus Gattii : Novel Candidate Antigens for Diagnosis

et al. 2013

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Section: Discussionmentioning

confidence: 85%

Immunoproteomics and Immunoinformatics Analysis of Cryptococcus Gattii : Novel Candidate Antigens for Diagnosis

et al. 2013

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“…Only three M. anisopliae chitinases were experimentally identified thus far in culture supernatants: CHIT42 (ChiMaA1), CHI2 (ChiMaB1) and CHIT30 (ChiMaB2) [25], [66]. Santi et al [67] detected chitinase activity in M. anisopliae intact conidial extracts, indicating that some chitinases may be localized at the spore surface. Chitinase CHIT42 (ChiMaA1) was also detected at the spore surface by immunoproteomic analysis [68].…”

Section: Discussionmentioning

confidence: 99%

Genomic Analyses and Transcriptional Profiles of the Glycoside Hydrolase Family 18 Genes of the Entomopathogenic Fungus Metarhizium anisopliae

et al. 2014

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Fungal chitin metabolism involves diverse processes such as metabolically active cell wall maintenance, basic nutrition, and different aspects of virulence. Chitinases are enzymes belonging to the glycoside hydrolase family 18 (GH18) and 19 (GH19) and are responsible for the hydrolysis of β-1,4-linkages in chitin. This linear homopolymer of N-acetyl-β-D-glucosamine is an essential constituent of fungal cell walls and arthropod exoskeletons. Several chitinases have been directly implicated in structural, morphogenetic, autolytic and nutritional activities of fungal cells. In the entomopathogen Metarhizium anisopliae, chitinases are also involved in virulence. Filamentous fungi genomes exhibit a higher number of chitinase-coding genes than bacteria or yeasts. The survey performed in the M. anisopliae genome has successfully identified 24 genes belonging to glycoside hydrolase family 18, including three previously experimentally determined chitinase-coding genes named chit1, chi2 and chi3. These putative chitinases were classified based on domain organization and phylogenetic analysis into the previously described A, B and C chitinase subgroups, and into a new subgroup D. Moreover, three GH18 proteins could be classified as putative endo-N-acetyl-β-D-glucosaminidases, enzymes that are associated with deglycosylation and were therefore assigned to a new subgroup E. The transcriptional profile of the GH18 genes was evaluated by qPCR with RNA extracted from eight culture conditions, representing different stages of development or different nutritional states. The transcripts from the GH18 genes were detected in at least one of the different M. anisopliae developmental stages, thus validating the proposed genes. Moreover, not all members from the same chitinase subgroup presented equal patterns of transcript expression under the eight distinct conditions studied. The determination of M. anisopliae chitinases and ENGases and a more detailed study concerning the enzymes’ roles in morphological or nutritional functions will allow comprehensive insights into the chitinolytic potential of this highly infective entomopathogenic fungus.

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“…The participation of proteases and chitinases in the infection process has been shown previously (Gillespie et al 1998;Dutra et al 2004;da Silva et al 2005;Santi et al 2009;Santi et al 2010b). The availability of the Agrobacteriummediated transformation system for constructing functional mutants of selected genes (Staats et al 2007) has made it possible to show that the interruption of a single chitinase gene results in the decreased efficiency of insect infection (Boldo et al 2009).…”

Section: Introductionmentioning

confidence: 90%

The entomopathogen Metarhizium anisopliae can modulate the secretion of lipolytic enzymes in response to different substrates including components of arthropod cuticle

et al. 2010

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Metarhizium anisopliae host–pathogen interaction: differential immunoproteomics reveals proteins involved in the infection process of arthropods

Cited by 45 publications

References 49 publications

Immunoproteomics and Immunoinformatics Analysis of Cryptococcus Gattii : Novel Candidate Antigens for Diagnosis

Immunoproteomics and Immunoinformatics Analysis of Cryptococcus Gattii : Novel Candidate Antigens for Diagnosis

Genomic Analyses and Transcriptional Profiles of the Glycoside Hydrolase Family 18 Genes of the Entomopathogenic Fungus Metarhizium anisopliae

The entomopathogen Metarhizium anisopliae can modulate the secretion of lipolytic enzymes in response to different substrates including components of arthropod cuticle

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