The potential of antimicrobial peptides isolated from freshwater crayfish species in new drug development: A review

被引:18
作者
Punginelli, Diletta [1 ]
Schillaci, Domenico [1 ]
Mauro, Manuela [1 ]
Deidun, Alan [2 ]
Barone, Giampaolo [1 ]
Arizza, Vincenzo [1 ]
Vazzana, Mirella [1 ]
机构
[1] Univ Palermo, Dept Biol Chem & Pharmaceut Sci & Technol STEBICE, Via Archirafi 18, I-90123 Palermo, Italy
[2] Univ Malta, Fac Sci, Dept Geosci, MSD-2080 Msida, Malta
关键词
AMP; Antibiotic; Bioactive compound; Crustacea; Invertebrate; Pathogenic bacteria; RED SWAMP CRAYFISH; GRAM-NEGATIVE BACTERIA; C-TYPE LYSOZYME; FACTOR; 6; TRAF6; MOLECULAR-CLONING; INNATE IMMUNE; ANTILIPOPOLYSACCHARIDE FACTOR; ANTIBACTERIAL PEPTIDE; SYNDROME-VIRUS; LITOPENAEUS-VANNAMEI;
D O I
10.1016/j.dci.2021.104258
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
The much-publicised increased resistance of pathogenic bacteria to conventional antibiotics has focused research effort on the characterization of new antimicrobial drugs. In this context, antimicrobial peptides (AMPs) extracted from animals are considered a promising alternative to conventional antibiotics. In recent years, freshwater crayfish species have emerged as an important source of bioactive compounds. In fact, these invertebrates rely on an innate immune system based on cellular responses and on the production of important effectors in the haemolymph, such as AMPs, which are produced and stored in granules in haemocytes and released after stimulation. These effectors are active against both Gram-positive and Gram-negative bacteria. In this review, we summarise the recent progress on AMPs isolated from the several species of freshwater crayfish and their prospects for future pharmaceutical applications to combat infectious agents.
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页数:10
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共 180 条
[1]   Pathogen recognition and innate immunity [J].
Akira, S ;
Uematsu, S ;
Takeuchi, O .
CELL, 2006, 124 (04) :783-801
[2]   Molecular cloning, genomic organization and recombinant expression of a crustin-like antimicrobial peptide from black tiger shrimp Penaeus monodon [J].
Amparyup, Piti ;
Kondo, Hidehiro ;
Hirono, Ikuo ;
Aoki, Takashi ;
Tassanakajon, Anchalee .
MOLECULAR IMMUNOLOGY, 2008, 45 (04) :1085-1093
[3]   INFORMATION FOR THE DORSAL VENTRAL PATTERN OF THE DROSOPHILA EMBRYO IS STORED AS MATERNAL MESSENGER-RNA [J].
ANDERSON, KV ;
NUSSLEINVOLHARD, C .
NATURE, 1984, 311 (5983) :223-227
[4]   Cecropins, antibacterial peptides from insects and mammals, are potently fungicidal against Candida albicans [J].
Andrä, J ;
Berninghausen, O ;
Leippe, M .
MEDICAL MICROBIOLOGY AND IMMUNOLOGY, 2001, 189 (03) :169-173
[5]   Membrane permeability and antimicrobial kinetics of cecropin P1 against Escherichia coli [J].
Arcidiacono, Steven ;
Soares, Jason W. ;
Meehan, Alexa M. ;
Marek, Patrick ;
Kirby, Romy .
JOURNAL OF PEPTIDE SCIENCE, 2009, 15 (06) :398-403
[6]   Antimicrobial Peptides [J].
Bahar, Ali Adem ;
Ren, Dacheng .
PHARMACEUTICALS, 2013, 6 (12) :1543-1575
[7]  
Bíliková K, 2001, APIDOLOGIE, V32, P275, DOI 10.1051/apido:2001129
[8]   Proteins with whey-aicidic-protein motifs and cancer [J].
Bouchard, D ;
Morisset, D ;
Bourbonnais, Y ;
Tremblay, GM .
LANCET ONCOLOGY, 2006, 7 (02) :167-174
[9]   The interleukin-1 receptor/Toll-like receptor superfamily: signal generators for pro-inflammatory interleukins and microbial products [J].
Bowie, A ;
O'Neill, LAJ .
JOURNAL OF LEUKOCYTE BIOLOGY, 2000, 67 (04) :508-514
[10]   Gene characterisation, isoforms and recombinant expression of carcinin, an antibacterial protein from the shore crab, Carcinus maenas [J].
Brockton, Virginia ;
Hammond, John A. ;
Smith, Valerie J. .
MOLECULAR IMMUNOLOGY, 2007, 44 (05) :943-949