Molecular characterization of Nosema bombycis methionine aminopeptidase 2 (MetAP2) gene and evaluation of anti-microsporidian activity of Fumagilin-B in silkworm Bombyx mori

被引：11

作者：

Esvaran, Vijaya Gowri ^{[1
]}

Gupta, Tania ^{[1
]}

Nayaka, A. R. Narasimha ^{[2
]}

Sivaprasad, Vankadara ^{[2
]}

Ponnuvel, Kangayam M. ^{[1
]}

机构：

[1] Seribiotech Res Lab, Genom Div, Bangalore 560035, Karnataka, India

[2] Cent Sericulture Training & Res Inst, Silkworm Pathol Div, Mysore 570008, Karnataka, India

来源：

3 BIOTECH | 2018年 / 8卷 / 09期

关键词：

Microsporidiosis; MetAP2; Fumagillin; Nosema bombycis; Anti-microsporidian; METHIONINE AMINOPEPTIDASE; OVALICIN; ANGIOGENESIS; TNP-470; TARGET; TYPE-2;

D O I：

10.1007/s13205-018-1411-z

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Nosema bombycis is a spore-forming parasite causing microsporidiosis in silkworm Bombyx mori. Methionine aminopeptidase 2 (MetAP2), an essential gene of N. bombycis, is a target for the anti-microsporidian drug Fumagillin, an antibiotic derived from Aspergillus fumigatus. In this study, a 1077 bp full-length cDNA of the MetAP2 gene of N. bombycis was cloned and characterized. Furthermore, the expression study of the MetAP2 gene revealed a ubiquitous expression during all the developmental stages of the silkworm B. mori. The phylogenetic analysis of the MetAP2 gene of N. bombycis revealed the MetAP2 gene sequences to be highly conserved in nature. The present study also includes the validation of the anti-microsporidian drug Fumagillin against the MetAP2 gene of N. bombycis. The findings revealed that Fumagilin-B could also suppress the N. bombycis multiplication in the silkworm B. mori, thereby proving the therapeutic role of Fumagillin against microsporidian infection. This is the first-ever report regarding the characterization of the MetAP2 gene in the Indian isolate of N. bombycis and also towards the usage of Fumagillin in the control of microsporidiosis in B. mori.

引用

页数：8

共 19 条

[1] Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470 [J].

Alvarado, John Jeff ;

Nemkal, Anjana ;

Sauder, J. Michael ;

Russell, Marijane ;

Akiyoshi, Donna E. ;

Shi, Wuxian ;

Almo, Steven C. ;

Weiss, Louis M. .

MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 2009, 168 (02) :158-167

[2] Antimicrosporidial activities of fumagillin, TNP-470, ovalicin, and ovalicin derivatives in vitro and in vivo [J].

Didier, Peter J. ;

Phillips, Jennifer N. ;

Kuebler, Dorothy J. ;

Nasr, Mohamed ;

Brindley, Paul J. ;

Stovall, Mary E. ;

Bowers, Lisa C. ;

Didier, E. S. .

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2006, 50 (06) :2146-2155

[3] Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin [J].

Griffith, EC ;

Su, Z ;

Turk, BE ;

Chen, SP ;

Chang, YH ;

Wu, ZC ;

Biemann, K ;

Liu, JO .

CHEMISTRY & BIOLOGY, 1997, 4 (06) :461-471

[4] Treatment of microsporidiosis including albendazole [J].

Gross, U .

PARASITOLOGY RESEARCH, 2003, 90 (Suppl 1) :S14-S18

[5] The stability and effectiveness of fumagillin in controlling Nosema ceranae (Microsporidia) infection in honey bees (Apis mellifera) under laboratory and field conditions [J].

Higes, Mariano ;

Nozal, Maria J. ;

Alvaro, Ana ;

Barrios, Laura ;

Meana, Aranzazu ;

Martin-Hernandez, Raquel ;

Bernal, Jose L. ;

Bernal, Jose .

APIDOLOGIE, 2011, 42 (03) :364-377

[6] Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi [J].

Katinka, MD ;

Duprat, S ;

Cornillot, E ;

Méténier, G ;

Thomarat, F ;

Prensier, G ;

Barbe, V ;

Peyretaillade, E ;

Brottier, P ;

Wincker, P ;

Delbac, F ;

El Alaoui, H ;

Peyret, P ;

Saurin, W ;

Gouy, M ;

Weissenbach, J ;

Vivarès, CP .

NATURE, 2001, 414 (6862) :450-453

[7] Understanding the selectivity of fumagillin for the methionine aminopeptidase type II [J].

Klein, CDP ;

Folkers, G .

ONCOLOGY RESEARCH, 2003, 13 (12) :513-520

[8] MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment [J].

Kumar, S ;

Tamura, K ;

Nei, M .

BRIEFINGS IN BIOINFORMATICS, 2004, 5 (02) :150-163

[9] Structure of human methionine aminopeptidase-2 complexed with fumagillin [J].

Liu, SP ;

Widom, J ;

Kemp, CW ;

Crews, CM ;

Clardy, J .

SCIENCE, 1998, 282 (5392) :1324-1327

[10] The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase [J].

Lowther, WT ;

McMillen, DA ;

Orville, AM ;

Matthews, BW .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (21) :12153-12157

← 1 2 →