المؤلفون: Venugopalan, Lakshmi Prabha^{Aff1, Aff2}, Aimanianda, Vishukumar^{Aff3, Aff4}, Namperumalsamy, Venkatesh Prajna, Prajna, Lalitha, Kuppamuthu, Dharmalingam, Jayapal, Jeya Maheshwari^{Aff1, IDs00253023125594_cor6}

المصدر: Applied Microbiology and Biotechnology. :1-16

المؤلفون: Zhang, Maoge^{Aff1, Aff2, Aff3}, Wei, Qinglv^{Aff1, Aff2, Aff3}, Xia, Yuxian^{Aff1, Aff2, Aff3}, Jin, Kai^{Aff1, Aff2, Aff3}

المصدر: Current Genetics: Microorganisms and Organelles. 66(2):397-408

المؤلفون: Isabel Valsecchi, Emmanuel Stephen-Victor, Sarah Sze Wah Wong, Anupama Karnam, Margaret Sunde, J. Iñaki Guijarro, Borja Rodríguez de Francisco, Thomas Krüger, Olaf Kniemeyer, Gordon D. Brown, Janet A. Willment, Jean-Paul Latgé, Axel A. Brakhage, Jagadeesh Bayry, Vishukumar Aimanianda

المصدر: Journal of Fungi, Vol 6, Iss 3, p 151 (2020)

مصطلحات موضوعية: Aspergillus fumigatus, host–fungal interaction, conidial surface, RodAp, hydrophobin, disulfide bonds, Biology (General), QH301-705.5

الوصف: Immune inertness of Aspergillusfumigatus conidia is attributed to its surface rodlet-layer made up of RodAp, characterized by eight conserved cysteine residues forming four disulfide bonds. Earlier, we showed that the conserved cysteine residue point (ccrp) mutations result in conidia devoid of the rodlet layer. Here, we extended our study comparing the surface organization and immunoreactivity of conidia carrying ccrp-mutations with the RODA deletion mutant (∆rodA). Western blot analysis using anti-RodAp antibodies indicated the absence of RodAp in the cytoplasm of ccrp-mutant conidia. Immunolabeling revealed differential reactivity to conidial surface glucans, the ccrp-mutant conidia preferentially binding to α-(1,3)-glucan, ∆rodA conidia selectively bound to β-(1,3)-glucan; the parental strain conidia showed negative labeling. However, permeability of ccrp-mutants and ∆rodA was similar to the parental strain conidia. Proteomic analyses of the conidial surface exposed proteins of the ccrp-mutants showed more similarities with the parental strain, but were significantly different from the ∆rodA. Ccrp-mutant conidia were less immunostimulatory compared to ∆rodA conidia. Our data suggest that (i) the conserved cysteine residues are essential for the trafficking of RodAp and the organization of the rodlet layer on the conidial surface, and (ii) targeted point mutation could be an alternative approach to study the role of fungal cell-wall genes in host–fungal interaction.

وصف الملف: electronic resource

Relation: https://www.mdpi.com/2309-608X/6/3/151; https://doaj.org/toc/2309-608X

URL الوصول: https://doaj.org/article/0a7ad606191b4a8ea176a524647b608e

المؤلفون: Watanabe, Satoshi, Kumakura, Kazuo, Kato, Hideki, Iyozumi, Hiroyuki, Togawa, Masayuki, Nagayama, Kozo

المصدر: Journal of General Plant Pathology. October 2005 71(5):351-356

المؤلفون: Takeo, K., de Hoog, G. S., Miyaji, M., Nishimura, K.

المصدر: Antonie van Leeuwenhoek: International Journal of General and Molecular Microbiology. March 1995 68(1):51-55

المؤلفون: Vishukumar Aimanianda, Olaf Kniemeyer, Sarah Sze Wah Wong, Borja Rodríguez de Francisco, Isabel Valsecchi, J. Iñaki Guijarro, Margaret Sunde, Janet A. Willment, Jagadeesh Bayry, Emmanuel Stephen-Victor, Anupama Karnam, Gordon D. Brown, Thomas Krüger, Axel A. Brakhage, Jean-Paul Latgé

المساهمون: Aspergillus, Institut Pasteur [Paris], Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP), Mycologie moléculaire - Molecular Mycology, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), The University of Sydney, Plateforme technologique de RMN biologique - Biological NMR Technological Platform, Leibniz Institute for Natural Product Research and Infection Biology (Hans Knoell Institute), University of Exeter, This work was supported by ANR-DFG AfuINF, ANR HYDROPHOBIN (ANR-10-BLAN-1309), ANR FUNHYDRO (ANR-16S-CE110020-01) and DFG CRC/TR FungiNet 124 (210879364, projects A1 and Z2) grants. SSWW was supported by a postdoctoral fellowship by ANR-DFG grant and Pasteur-Roux-Cantarini fellowship. MS was supported by an Australian Research Council Discovery Project (DP150104227). AK was supported by a fellowship from La Fondation pour la Recherche Médicale (FDT201805005552)., ANR-10-BLAN-1309,HYDROPHOBIN,HYDROPHOBINE DES CONIDIES d'Aspergillus fumigatus : ANALYSE STRUCTURALE ET REPONSE IMMUNE(2010), ANR-16-CE11-0020,FUNHYDRO,Amyloïdes fonctionnels formés par les hydrophobines du pathogène fongique Aspergillus fumigatus(2016), Institut Pasteur [Paris] (IP), École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université Paris Cité (UPCité), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

المصدر: Journal of Fungi, Vol 6, Iss 151, p 151 (2020)
Journal of Fungi
Journal of Fungi, MDPI, 2020, 6 (3), pp.151. ⟨10.3390/jof6030151⟩
Volume 6
Issue 3
Journal of Fungi, 2020, 6 (3), pp.151. ⟨10.3390/jof6030151⟩

مصطلحات موضوعية: Microbiology (medical), hydrophobin, Hydrophobin, Aspergillus fumigatus, disulfide bonds, Plant Science, immunomodulation, Microbiology, Conidium, 03 medical and health sciences, Immunolabeling, Western blot, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], medicine, skin and connective tissue diseases, lcsh:QH301-705.5, Ecology, Evolution, Behavior and Systematics, 030304 developmental biology, 0303 health sciences, biology, medicine.diagnostic_test, 030306 microbiology, Chemistry, Point mutation, fungi, RodAp, biology.organism_classification, conidial surface, 3. Good health, host–fungal interaction, lcsh:Biology (General), Cytoplasm, Cysteine

الوصف: Immune inertness of Aspergillusfumigatus conidia is attributed to its surface rodlet-layer made up of RodAp, characterized by eight conserved cysteine residues forming four disulfide bonds. Earlier, we showed that the conserved cysteine residue point (ccrp) mutations result in conidia devoid of the rodlet layer. Here, we extended our study comparing the surface organization and immunoreactivity of conidia carrying ccrp-mutations with the RODA deletion mutant (∆rodA). Western blot analysis using anti-RodAp antibodies indicated the absence of RodAp in the cytoplasm of ccrp-mutant conidia. Immunolabeling revealed differential reactivity to conidial surface glucans, the ccrp-mutant conidia preferentially binding to &alpha
(1,3)-glucan, ∆rodA conidia selectively bound to &beta
(1,3)-glucan
the parental strain conidia showed negative labeling. However, permeability of ccrp-mutants and ∆rodA was similar to the parental strain conidia. Proteomic analyses of the conidial surface exposed proteins of the ccrp-mutants showed more similarities with the parental strain, but were significantly different from the ∆rodA. Ccrp-mutant conidia were less immunostimulatory compared to ∆rodA conidia. Our data suggest that (i) the conserved cysteine residues are essential for the trafficking of RodAp and the organization of the rodlet layer on the conidial surface, and (ii) targeted point mutation could be an alternative approach to study the role of fungal cell-wall genes in host&ndash
fungal interaction.

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::640bed0b702a202eba0a9e1cd36c58e2
https://doi.org/10.3390/jof6030151

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