Characterization of an immunogenic cellulase secreted by Cryptococcus pathogens.
Animals
Carboxymethylcellulose Sodium
/ metabolism
Cellulase
/ chemistry
Cryptococcosis
/ immunology
Cryptococcus
/ enzymology
Cryptococcus neoformans
/ enzymology
Culture Media, Conditioned
Cytokines
/ immunology
Fungal Proteins
/ chemistry
Immunization
Mice
Molecular Weight
Recombinant Proteins
/ chemistry
Th1 Cells
/ immunology
cellulase
cryptococcal infection
immune responses
Journal
Medical mycology
ISSN: 1460-2709
Titre abrégé: Med Mycol
Pays: England
ID NLM: 9815835
Informations de publication
Date de publication:
10 Nov 2020
10 Nov 2020
Historique:
received:
28
11
2019
revised:
20
02
2020
accepted:
25
02
2020
pubmed:
5
4
2020
medline:
26
5
2021
entrez:
5
4
2020
Statut:
ppublish
Résumé
Members of the C. neoformans/C. gattiii species complex are an important cause of serious humans infections, including meningoencephalitis. We describe here a 45 kDa extracellular cellulase purified from culture supernatants of C. neoformans var. neoformans. The N-terminal sequence obtained from the purified protein was used to isolate a clone containing the full-length coding sequence from a C. neoformans var. neoformans (strain B-3501A) cDNA library. Bioinformatics analysis indicated that this gene is present, with variable homology, in all sequenced genomes of the C. neoformans/C. gattii species complex. The cDNA clone was used to produce a recombinant 45 kDa protein in E. coli that displayed the ability to convert carboxymethyl cellulose and was therefore designated as NG-Case (standing for Neoformans Gattii Cellulase). To explore its potential use as a vaccine candidate, the recombinant protein was used to immunize mice and was found capable of inducing T helper type 1 responses and delayed-type hypersensitivity reactions, but not immune protection against a highly virulent C. neoformans var grubii strain. These data may be useful to better understand the mechanisms underlying the ability C. neoformans/C. gattii to colonize plant habitats and to interact with the human host during infection.
Identifiants
pubmed: 32246714
pii: 5815798
doi: 10.1093/mmy/myaa012
doi:
Substances chimiques
Culture Media, Conditioned
0
Cytokines
0
Fungal Proteins
0
Recombinant Proteins
0
Cellulase
EC 3.2.1.4
Carboxymethylcellulose Sodium
K679OBS311
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1138-1148Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of The International Society for Human and Animal Mycology.