Plant α-amylase inhibitors and their interaction with insect α-amylases -: Structure, function and potential for crop protection

被引:370
作者
Franco, OL
Rigden, DJ
Melo, FR
Grossi-de-Sá, MF
机构
[1] Cenargen Embrapa, Ctr Nacl Recursos Genet & Biotecnol, Lab 05, BR-70770900 Brasilia, DF, Brazil
[2] Univ Catolica Brasilia, Brasilia, DF, Brazil
[3] Dept Biol Celular, Brasilia, DF, Brazil
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 2002年 / 269卷 / 02期
关键词
alpha-amylase inhibitors; knottin-like; lectin-like; thaumatin-like; Kunitz; cereal-type; bean weevils; bifunctional inhibitors;
D O I
10.1046/j.0014-2956.2001.02656.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Insect pests and pathogens (fungi, bacteria and viruses) are responsible for severe crop tosses. Insects feed directly on the plant tissues, while the pathogens lead to damage or death of the plant. Plants have evolved a certain degree of resistance through the production of defence compounds, which may be aproteic, e.g. antibiotics, alkaloids, terpenes, cyanogenic glucosides or proteic, e.g. chitinases, beta-1,3-glucanases, lectins, arcelins, vicilins, system ins and enzyme inhibitors. The enzyme inhibitors impede digestion through their action on insect gut digestive alpha-amylases and proteinases, which play a key role in the digestion of plant starch and proteins. The natural defences of crop plants may be improved through the use of transgenic technology. Current research in the area focuses particularly on weevils as these are highly dependent on starch for their energy supply. Six different alpha-amylase inhibitor classes, lectin-like, knottin-like, cereal-type, Kunitz-like, gamma-purothionin-like and thaumatin-like could be used in pest control. These classes of inhibitors show remarkable structural variety leading to different modes of inhibition and different specificity profiles against diverse alpha-amylases. Specificity of inhibition is an important issue as the introduced inhibitor must not adversely affect the plant's own alpha-amylases, nor the nutritional value of the crop. Of particular interest are some bifunctional inhibitors with additional favourable properties, such as proteinase inhibitory activity or chitinase activity. The area has benefited from the recent determination of many structures of alpha-amylases, inhibitors and complexes. These structures highlight the remarkable variety in structural modes of alpha-amylase inhibition. The continuing discovery of new classes of alpha-amylase inhibitor ensures that exciting discoveries remain to be made. In this review, we summarize existing knowledge of insect alpha-amylases, plant alpha-amylase inhibitors and their interaction. Positive results recently obtained for transgenic plants and future prospects in the area are reviewed.
引用
收藏
页码:397 / 412
页数:16
相关论文
共 165 条
[1]   Antifungal activity of tobacco osmotin has specificity and involves plasma membrane permeabilization [J].
Abad, LR ;
DUrzo, MP ;
Liu, D ;
Narasimhan, ML ;
Reuveni, M ;
Zhu, JK ;
Niu, XM ;
Singh, NK ;
Hasegawa, PM ;
Bressan, RA .
PLANT SCIENCE, 1996, 118 (01) :11-23
[2]   ARGININE IS ESSENTIAL FOR THE ALPHA-AMYLASE INHIBITORY ACTIVITY OF THE ALPHA-AMYLASE/SUBTILISIN INHIBITOR (BASI) FROM BARLEY-SEEDS [J].
ABE, J ;
SIDENIUS, U ;
SVENSSON, B .
BIOCHEMICAL JOURNAL, 1993, 293 :151-155
[3]   STABILITY AND KINETICS OF A BIFUNCTIONAL AMYLASE TRYPSIN-INHIBITOR [J].
ALAGIRI, S ;
SINGH, TP .
BIOCHIMICA ET BIOPHYSICA ACTA, 1993, 1203 (01) :77-84
[4]   Substrate-inhibitor interactions in the kinetics of α-amylase inhibition by Ragi α-amylase/trypsin inhibitor (RATI) and its various N-terminal fragments [J].
Alam, N ;
Gourinath, S ;
Dey, S ;
Srinivasan, A ;
Singh, TP .
BIOCHEMISTRY, 2001, 40 (14) :4229-4233
[5]  
[Anonymous], 1991, INT REV CYTOL
[6]   PURIFICATION AND CHARACTERIZATION OF AN INSECT ALPHA-AMYLASE INHIBITOR ENDOCHITINASE FROM SEEDS OF JOB TEARS (COIX-LACHRYMA-JOBI) [J].
ARY, MB ;
RICHARDSON, M ;
SHEWRY, PR .
BIOCHIMICA ET BIOPHYSICA ACTA, 1989, 999 (03) :260-266
[7]   The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family [J].
Batalia, MA ;
Monzingo, AF ;
Ernst, S ;
Roberts, W ;
Robertus, JD .
NATURE STRUCTURAL BIOLOGY, 1996, 3 (01) :19-23
[8]   Structural determinants of the bifunctional corn Hageman factor inhibitor:: X-ray crystal structure at 1.95 Å resolution [J].
Behnke, CA ;
Yee, VC ;
Le Trong, I ;
Pedersen, LC ;
Stenkamp, RE ;
Kim, SS ;
Reeck, GR ;
Teller, DC .
BIOCHEMISTRY, 1998, 37 (44) :15277-15288
[9]   SYNCHROTRON X-RAY DATA-COLLECTION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL-STRUCTURE OF PROTEINASE-K AT 1.5-A-RESOLUTION [J].
BETZEL, C ;
PAL, GP ;
SAENGER, W .
ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE, 1988, 44 :163-172
[10]   ACARBOSE, A NEW ENTITY IN THE TREATMENT OF DIABETES [J].
BISCHOFF, H ;
AHR, HJ ;
SCHMIDT, D ;
STOLTEFUSS, J .
NACHRICHTEN AUS CHEMIE TECHNIK UND LABORATORIUM, 1994, 42 (11) :1119-+