Characteristics and antifungal activity of a chitin binding protein fromGinkgo biloba

FEBS Letters ◽  
2000 ◽  
Vol 478 (1-2) ◽  
pp. 123-126 ◽  
Author(s):  
Xu Huang ◽  
Wei-jun Xie ◽  
Zhen-zhen Gong
2019 ◽  
Vol 26 (6) ◽  
pp. 414-422
Author(s):  
Jia Liu ◽  
Ping Song ◽  
Jie Zhang ◽  
Ziyan Nangong ◽  
Xiaobei Liu ◽  
...  

Background: Genome sequence analysis (GenBank access No.: FN667742.1) shows that Xenorhabdus nematophila ATCC19061 contains one gene (Xn-cbp) encoding chitin binding protein (Xn-CBP). Objective: The present work aims to clarify the characteristics and function of Xn-CBP from X. nematophila HB310. Methods: In this study, the Xn-cbp gene was cloned and expressed in Escherichia coli BL21 (DE3). Substrate binding assays were performed to explain the ability of Xn-CBP combined with the polysaccharide. The insecticidal toxicity of Xn-CBP against the second-instar larvae of Helicoverpa armigera was determined by feeding method. Besides, the antifungal activity of Xn-CBP against Coniothyrium diplodiella, Verticillium dahlia, and Fusarium oxysporum was tested by spore germination assay and hyphal extension assay. Results: Xn-CBP encoded 199 amino acids with a calculated mass of 28 kDa, which contained a signal peptide and a chitin binding domain. The Bmax and Kd values of Xn-CBP to colloidal chitin were 2.46 and 4.08, respectively. Xn-CBP had insecticidal activity against the H. armigera with a growth inhibition rate of 84.08%. Xn-CBP had the highest spore germination inhibitory effect on C. diplodiella with the inhibition rate of 83.11%. The hyphal growth inhibition rate of Xn-CBP to F. oxysporum, 41.52%, was higher than the other two fungi. Conclusion: The Xn-CBP had the highest binding ability to colloidal chitin and it showed insecticidal activity and antifungal activity. The present study laid a foundation for further exploitation and utilization of X. nematophila.


1999 ◽  
Vol 181 (24) ◽  
pp. 7421-7429 ◽  
Author(s):  
Christiane Bormann ◽  
Daniel Baier ◽  
Ingmar Hörr ◽  
Claudia Raps ◽  
Jürgen Berger ◽  
...  

ABSTRACT The afp1 gene, which encodes the antifungal protein AFP1, was cloned from nikkomycin-producing Streptomyces tendae Tü901, using a nikkomycin-negative mutant as a host and screening transformants for antifungal activity againstPaecilomyces variotii in agar diffusion assays. The 384-bpafp1 gene has a low G+C content (63%) and a transcription termination structure with a poly(T) region, unusual attributes forStreptomyces genes. AFP1 was purified from culture filtrate of S. tendae carrying the afp1 gene on the multicopy plasmid pIJ699. The purified protein had a molecular mass of 9,862 Da and lacked a 42-residue N-terminal peptide deduced from the nucleotide sequence. AFP1 was stable at extreme pH values and high temperatures and toward commercial proteinases. AFP1 had limited similarity to cellulose-binding domains of microbial plant cell wall hydrolases and bound to crab shell chitin, chitosan, and cell walls ofP. variotii but showed no enzyme activity. The biological activity of AFP1, which represents the first chitin-binding protein from bacteria exhibiting antifungal activity, was directed against specific ascomycetes, and synergistic interaction with the chitin synthetase inhibitor nikkomycin inhibited growth ofAspergillus species. Microscopy studies revealed that fluorescein-labeled AFP1 strongly bound to the surface of germinated conidia and to tips of growing hyphae, causing severe alterations in cell morphogenesis that gave rise to large spherical conidia and/or swollen hyphae and to atypical branching.


2021 ◽  
Vol 9 (4) ◽  
pp. 757
Author(s):  
Qing-Mei Li ◽  
Ying-Li Zhou ◽  
Zhan-Fei Wei ◽  
Yong Wang

Bdellovibrionota is composed of obligate predators that can consume some Gram-negative bacteria inhabiting various environments. However, whether genomic traits influence their distribution and marine adaptation remains to be answered. In this study, we performed phylogenomics and comparative genomics studies using 132 Bdellovibrionota genomes along with five metagenome-assembled genomes (MAGs) from deep sea zones. Four phylogenetic groups, Oligoflexia, Bdello-group1, Bdello-group2 and Bacteriovoracia, were revealed by constructing a phylogenetic tree, of which 53.84% of Bdello-group2 and 48.94% of Bacteriovoracia were derived from the ocean. Bacteriovoracia was more prevalent in deep sea zones, whereas Bdello-group2 was largely distributed in the epipelagic zone. Metabolic reconstruction indicated that genes involved in chemotaxis, flagellar (mobility), type II secretion system, ATP-binding cassette (ABC) transporters and penicillin-binding protein were necessary for the predatory lifestyle of Bdellovibrionota. Genes involved in glycerol metabolism, hydrogen peroxide (H2O2) degradation, cell wall recycling and peptide utilization were ubiquitously present in Bdellovibrionota genomes. Comparative genomics between marine and non-marine Bdellovibrionota demonstrated that betaine as an osmoprotectant is probably widely used by marine Bdellovibrionota, and all the marine genomes have a number of genes for adaptation to marine environments. The genes encoding chitinase and chitin-binding protein were identified for the first time in Oligoflexia, which implied that Oligoflexia may prey on a wider spectrum of microbes. This study expands our knowledge on adaption strategies of Bdellovibrionota inhabiting deep seas and the potential usage of Oligoflexia for biological control.


2008 ◽  
Vol 150 (1) ◽  
pp. 97-111 ◽  
Author(s):  
T. Santi-Gadelha ◽  
B. A. M. Rocha ◽  
C. C. Oliveira ◽  
K. S. Aragão ◽  
E. S. Marinho ◽  
...  

2020 ◽  
Vol 78 (1) ◽  
Author(s):  
Sajad Rashidi ◽  
Kurosh Kalantar ◽  
Celia Fernandez-Rubio ◽  
Enayat Anvari ◽  
Paul Nguewa ◽  
...  

ABSTRACT Leishmaniasis includes a broad spectrum of pathological outcomes in humans caused by protozoan parasites from the genus Leishmania. In recent years, proteomic techniques have introduced novel proteins with critical functions in Leishmania parasites. Based on our report of a Chitin binding protein (CBP) in our previous immunoproteomic study, this article suggests that CBP might be an RNA binding protein (RBP) in Leishmania parasites. RBPs, as key regulatory factors, have a role in post-transcriptional gene regulation. The presence of RBPs in Leishmania parasites has not been considered so far; however, this study aims to open a new venue regarding RBPs in Leishmania parasites. Confirming CBP as an RBP in Leishmania parasites, exploring other RBPs and their functions might lead to interesting issues in leishmaniasis. In fact, due to the regulatory role of RBPs in different diseases including cancers and their further classification as therapeutic targets, the emerging evaluation of CBP and RBPs from Leishmania parasites may allow the discovery of novel and effective drugs against leishmaniasis.


FEBS Letters ◽  
2006 ◽  
Vol 580 (6) ◽  
pp. 1541-1546 ◽  
Author(s):  
Laurence V. Bindschedler ◽  
Julian P. Whitelegge ◽  
David J. Millar ◽  
G. Paul Bolwell

2010 ◽  
Vol 5 (1) ◽  
pp. 117-119 ◽  
Author(s):  
Finn L. Aachmann ◽  
Vincent G. H. Eijsink ◽  
Gustav Vaaje-Kolstad

2003 ◽  
Vol 96 (1-2) ◽  
pp. 113-122 ◽  
Author(s):  
Zhaofei Li ◽  
Chongbi Li ◽  
Kai Yang ◽  
Lihua Wang ◽  
Chong Yin ◽  
...  

FEBS Journal ◽  
2009 ◽  
Vol 276 (8) ◽  
pp. 2402-2415 ◽  
Author(s):  
Gustav Vaaje-Kolstad ◽  
Anne C. Bunaes ◽  
Geir Mathiesen ◽  
Vincent G. H. Eijsink

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