Defensins - Components of the innate immune system in plants

被引:371
作者
Lay, FT [1 ]
Anderson, MA [1 ]
机构
[1] La Trobe Univ, Dept Biochem, Bundoora, Vic 3086, Australia
关键词
defensin; antimicrobial; antifungal; CS alpha beta motif; innate immunity; prodomain; defense;
D O I
10.2174/1389203053027575
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
Plant defensins are small (c.a. 5 kDa), basic, cysteine-rich proteins with antimicrobial activities. They are ubiquitous in plants and form part of the innate immunity arsenal. Plant defensins are encoded by small multigene families and are expressed in various plant tissues, but are best characterized in seeds. They are typically produced as preproteins, however, a small subset are produced as larger precursors with C-terminal prodomains. To date, the three-dimensional solution structures of seven seed- and two floral-derived defensins have been elucidated by H-1-NMR spectroscopy. Despite limited amino acid sequence identities, these defensins have comparable global folds with features that are characteristic of the cysteine-stabilized alphabeta (CSalphabeta) motif. Interestingly, their structures are remarkably similar to those of insect defensins and scorpion toxins. Functionally, these proteins exhibit a diverse array of biological activities, although they all serve a common function as defenders of their hosts. This review describes the distribution, biosynthesis, structure, function and mode of action of plant defensins and reflects on their potential in agribiotechnological applications.
引用
收藏
页码:85 / 101
页数:17
相关论文
共 188 条
  • [1] Characterization of two novel defense peptides from pea (Pisum sativum) seeds
    Almeida, MS
    Cabral, KMS
    Zingali, RB
    Kurtenbach, E
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2000, 378 (02) : 278 - 286
  • [2] cDNA cloning and heterologous expression of functional cysteine-rich antifungal protein Psd1 in the yeast Pichia pastoris
    Almeida, MS
    Cabral, KS
    de Medeiros, LN
    Valente, AP
    Almeida, FCL
    Kurtenbach, E
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2001, 395 (02) : 199 - 207
  • [3] Solution structure of Pisum sativum defensin 1 by high resolution NMR:: Plant defensins, identical backbone with different mechanisms of action
    Almeida, MS
    Cabral, KMS
    Kurtenbach, E
    Almeida, FCL
    Valente, AP
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2002, 315 (04) : 749 - 757
  • [4] [Anonymous], 1999, Plant Physiol, V120, P633, DOI 10.1104/pp.120.2.633
  • [5] Activation of Paneth cell α-defensins in mouse small intestine
    Ayabe, T
    Satchell, DP
    Pesendorfer, P
    Tanabe, H
    Wilson, CL
    Hagen, SJ
    Ouellette, AJ
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (07) : 5219 - 5228
  • [6] Human β-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung
    Bals, R
    Wang, XR
    Wu, ZR
    Freeman, T
    Bafna, V
    Zasloff, M
    Wilson, JM
    [J]. JOURNAL OF CLINICAL INVESTIGATION, 1998, 102 (05) : 874 - 880
  • [7] Bloch C, 1998, PROTEINS, V32, P334, DOI 10.1002/(SICI)1097-0134(19980815)32:3<334::AID-PROT9>3.0.CO
  • [8] 2-H
  • [9] A NEW FAMILY OF SMALL (5 KDA) PROTEIN INHIBITORS OF INSECT ALPHA-AMYLASES FROM SEEDS OR SORGHUM (SORGHUM-BICOLOR (L) MOENCH) HAVE SEQUENCE HOMOLOGIES WITH WHEAT GAMMA-PUROTHIONINS
    BLOCH, C
    RICHARDSON, M
    [J]. FEBS LETTERS, 1991, 279 (01) : 101 - 104
  • [10] THE ROLE OF THIONINS IN PLANT-PROTECTION
    BOHLMANN, H
    [J]. CRITICAL REVIEWS IN PLANT SCIENCES, 1994, 13 (01) : 1 - 16