Computational modeling and functional characterization of a GgChi: A class III chitinase from corms of Gladiolus grandiflorus.

Autor: Rafiq M; Botany Division, Institute of Pure and Applied Biology, Bahauddin Zakariya University, Multan, Pakistan., Hussain A; TUM School of Life Sciences Weihenstephan, Technical University of Munich, Germany., Shah KH; Botany Division, Institute of Pure and Applied Biology, Bahauddin Zakariya University, Multan, Pakistan., Saeed Q; Department of Entomology, Bahauddin Zakariya University, Multan, Pakistan., Sial MU; Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, PR China., Ali Z; Department of Biosciences, COMSATS University Islamabad, Park Road, Islamabad, Pakistan., Buck F; Institute of Clinical Chemistry, University Medical Centre Hamburg-Eppendorf, Hamburg, Germany., Goodman RE; Food Allergy Research and Resource Program, Department of Food Science & Technology, University of Nebraska-Lincoln, Lincoln, USA., Khaliq B; Botany Division, Institute of Pure and Applied Biology, Bahauddin Zakariya University, Multan, Pakistan., Ishaq U; Department of Botany, The Women University, Multan, Pakistan., Baig MA; Botany Division, Institute of Pure and Applied Biology, Bahauddin Zakariya University, Multan, Pakistan., Munawar A; Department of Chemistry, Faculty of Natural Sciences, Humanities & Islamic Studies, University of Engineering and Technology, Lahore, Pakistan., Mahmood S; Botany Division, Institute of Pure and Applied Biology, Bahauddin Zakariya University, Multan, Pakistan., Akrem A; Botany Division, Institute of Pure and Applied Biology, Bahauddin Zakariya University, Multan, Pakistan. Electronic address: ahmedakrem@bzu.edu.pk.
Jazyk: angličtina
Zdroj: The Kaohsiung journal of medical sciences [Kaohsiung J Med Sci] 2018 Dec; Vol. 34 (12), pp. 673-683. Date of Electronic Publication: 2018 Oct 12.
DOI: 10.1016/j.kjms.2018.08.003
Abstrakt: The present study describes the predicted model and functional characterization of an endochitinase (30 kDa) from corms of Gladiolus grandiflorus. ESI-QTOF-MS generated peptide showed 96% sequence homology with family 18, Class III acidic endochitinase of Gladiolus gandavensis. Purified G. grandiflorus chitinase (GgChi) hydrolyzed 4-methylumbelliferyl β-d-N,N',N''-triacetylchitotriose substrate showing specific endochitinase activity. Since no structural details of GgChi were available in the Protein Data Bank (PDB), a homology model was predicted using the coordinate information of Crocus vernus chitinase (PDB ID: 3SIM). Ramachandran plot indicated 84.5% in most favored region, 14.8% in additional and 0.6% in generously allowed region while no residue in disallowed region. The predicted structure indicated a highly conserved (β/α) 8 (TIM barrel) structure similar to the family 18, class III chitinases. The GgChi also showed sequence and structural homologies with other active chitinases. The GgChi (50 μg/disc) showed no antibacterial activity, but did provide mild growth inhibition of phytopathogenic fungus Fusarium oxysporum at a concentration of 500 μg/well Similarly, insect toxicity bioassays of GgChi (50 μg) against nymphs of Bemisia tabaci showed 14% reduction in adult emergence and 14% increase in mortality rate in comparison to control values. The GgChi (1.5 mg) protein showed significant reduction in a population of flour beetle (Tribolium castaneum) after 35 days, but lower reactivity against rice weevil (Sitophilus oryzae). The results of this study provide detai.led insight on functional characterization of a family 18 class III acidic plant endochitinase.
(Copyright © 2018. Published by Elsevier Taiwan LLC.)
Databáze: MEDLINE
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