Molecular Characterization and Gene Expression Profiling ... - CUSAT

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1.7.13.2 Introduction of peptide antibiotics to the market Chapter 1 Due to the increasing interests of AMPs, many companies are making efforts to introduce the AMP products to the market. Natural AMPs have potential application in food preservation as they specifically kill microbial cells by destroying their unique membranes. LAB bacteriocins have well- documented lethal activity against food-borne pathogens and spoilage microorganisms (Cleveland et al., 2001), and can play a vital role in the design and application of food preservation technology (Leistner and Gorris, 1995; Montville and Winkowski, 1997). Currently, nisin is approved as a food preservative in more than 40 countries worldwide (Delves- Broughton, 1990) and the use of pediocin PA-1 is covered by several European and US patents (Vandenbergh et al., 1989). Both nisin and pediocin PA-1 have applications in dairy and canned products (Leisner et al., 1996; Montville and Winkowski, 1997). Magainin Pharmaceuticals have taken the α-helical magainin variant peptide MSI-78 into phase-III clinical trials in studies of efficacy against polymicrobic foot-ulcer infections in diabetes. Applied Microbiology has initiated a trial testing the efficacy of the bacterial lantibiotic peptide nisin against Helicobacter pylori stomach ulcers. Iseganan (IB-367, Intrabiotics, Mountain View, CA, USA), a protegrin derivative (Mosca et al., 2000), has passed phase II clinical trials for application against oral mucositis successfully and the company has announced plans to launch Phase II/III clinical study to investigate iseganan HCl (Giles et al., 2002) in the prevention of ventilator-associated pneumonia (VAP). Another formulation of this company, iseganan HCl solution for inhalation, has completed phase I clinical trials in cystic fibrosis patients. Other companies, for examples, Periodontix Inc. (Watertown, MA, USA) has entered phase I clinical trials for the application of a histatin-derived peptide against oral candidiasis and Trimeris (Durham, NC, USA) has successfully completed a phase II clinical Molecular Characterization and Gene Expression Profiling of Antimicrobial Peptides in Penaeid Shrimps 88
Chapter 1 trial, in which peptide T-20 (Su et al., 1999; Cohen et al., 2002; Wei et al., 2002) reduced the viral load of HIV-infected patients with up to 97%. Also Demegen (Pittsburgh, PA, USA) has successfully completed animal studies with peptide D2A21 (Robertson et al., 1998) as therapeutic for several types of cancer and has been developing this peptide gel formulation as a wound healing product to treat infected burns and wounds. Demegen’s P113L (histatin 5 fragment) Oral Rinse exhibits significant binding to oral mucosal membranes and has an excellent human safety profile in over 400 treated patients. Another product of Demegen, P113D derived from histatins (Sajjan et al., 2001), had been granted orphan drug status for the treatment of cystic fibrosis infections. Interestingly, a number of evidence has shown efficacy of some AMPs against systemic infections, including α-helical-peptide (SMAP29) efficacy against P. aeruginosa peritoneal infections, β-sheet- protegrin efficacy against methicillin-resistant S. aureus (MASA), vancomycin-resistant Enterococcus faecalis (VRE) and P. aeruginosa infections, and indolicidin in liposomal formulation against Aspergillus fungal infections (Ahmad et al., 1995; Steinberg et al., 1997; Saiman et al., 2001). Entomed (Illkirch, France)’s product, heliomicin (Lamberty et al., 2001) for systemic antifungal treatment is under preclinical stage. Human lactoferricin (AM Pharma, Bunnik, Netherland) and bactericidal/permeability-increasing protein (Xoma, Berkeley, CA, USA, Gray et al., 1989) have also been proved to have potential for systemic applications. Indeed, Neuprex, a systemic formulation of the recombinant BPI-derived peptide rBPI 21 (Xoma Corp., Berkeley, CA, USA, Horwitz et al., 1996), has proven to be very effective in treatment of meningococcal sepsis in phase II/III clinical trials and more than 1000 patients have received NEUPREX in clinical studies without any safety concerns. Other major companies marketing AMPs include Novozyme (http://www.novozymes.com/en) and Micrologix (Migenix; http://www.migenix.com). Molecular Characterization and Gene Expression Profiling of Antimicrobial Peptides in Penaeid Shrimps 89
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Molecular Characterization and Gene
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Declaration I hereby do declare tha
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Acknowledgements This work was carr
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My Seniors, Dr. Annies Joseph, Dr.
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Contents Title Page Nos. 1 General
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in response to WSSV challenge 252-2
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α-2M Alpha-2-Macroglobulin ALF Ant
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ppA Prophenoloxidase-Activating Enz
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1.1 Introduction Chapter 1 Aquacult
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Chapter 1 the giant tiger shrimp (P
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Common names: Chapter 1 Giant tiger
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1.3.1. Diseases Chapter 1 Diseases
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Lymphoidal parvo-like virus (LPV) B
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Chapter 1 and protective occlusion
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Chapter 1 small brown masses in the
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1.4.6. Natural epidemics Chapter 1
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Chapter 1 can differentiate WSSV-in
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1.5.1.1. Probiotics Chapter 1 Alter
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Chapter 1 tried in P. monodon, resu
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Chapter 1 The first and essential i
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Chapter 1 1998). The innate immunit
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1.6.1 Haemocytes Chapter 1 The haem
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Chapter 1 In crustaceans, the sheet
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Chapter 1 Theopold et al., 2002). C
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Chapter 1 kill/remove the invading
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Chapter 1 forming complexes with a
Page 53 and 54: 1.7 Antimicrobial Peptides (AMPs) 1
Page 55 and 56: Chapter 1 the response is very fast
Page 57 and 58: Chapter 1 Hirsch, 1947). While they
Page 59 and 60: Chapter 1 AMPs to various degrees u
Page 61 and 62: 1.7.5 Biological activity Chapter 1
Page 63 and 64: Chapter 1 including the microbes as
Page 65 and 66: Tachyplesin I Chapter 1 Crustacea P
Page 67 and 68: Anionic and cationic peptides that
Page 69 and 70: Anionic and Cationic AMPs with cyst
Page 71 and 72: Chapter 1 Fig. 1.7. Structural clas
Page 73 and 74: Chapter 1 Group III: Linear peptide
Page 75 and 76: Chapter 1 through regular processes
Page 77 and 78: Chapter 1 ultimately signal to tran
Page 79 and 80: Chapter 1 divalent polyanionic cati
Page 81 and 82: Chapter 1 type of transmembrane por
Page 83 and 84: Chapter 1 other intracellular targe
Page 85 and 86: Chapter 1 Apidaecin, a short, proli
Page 87 and 88: Chapter 1 Hultmark, 1987; Gennaro a
Page 89 and 90: Chapter 1 quite opposite characteri
Page 91 and 92: Chapter 1 depletion of mitochondria
Page 93 and 94: Chapter 1 conformations adopted by
Page 95 and 96: Chapter 1 receptor may be a potenti
Page 97 and 98: Chapter 1 exposure to their targets
Page 99 and 100: Chapter 1 generating a rich spectru
Page 101 and 102: Chapter 1 by enkelytin (Goumon et a
Page 103: Lactoferricin Cow Mastitis control
Page 107 and 108: Chapter 1 a too limited spectrum to
Page 109 and 110: Chapter 1 number of research groups
Page 111 and 112: CHAPTER-2 Molecular Characterizatio
Page 113 and 114: Chapter 2 interaction with negative
Page 115 and 116: Chapter 2 inhibit the endotoxin or
Page 117 and 118: Chapter 2 structure be modified to
Page 119 and 120: Chapter 2 and the region might be l
Page 121 and 122: Chapter 2 been made of the spectra
Page 123 and 124: Chapter 2 their discovery and initi
Page 125 and 126: Chapter 2 terminal pyroglutamic aci
Page 127 and 128: Chapter 2 One can assume that the p
Page 129 and 130: Chapter 2 by degranulation into the
Page 131 and 132: 2.2. Materials and Methods 2.2.1. E
Page 133 and 134: Chapter 2 washed by adding 1 ml 75
Page 135 and 136: Chapter 2 entry of recombinant DNA
Page 137 and 138: Chapter 2 and the deduced amino aci
Page 139 and 140: Chapter 2 Fenneropenaeus, Litopenae
Page 141 and 142: 2.3.1.3. Crustin-1 (GQ334395) Chapt
Page 143 and 144: 2.3.1.3.5. Phylogenetic analysis of
Page 145 and 146: Chapter 2 sequence also showed high
Page 147 and 148: Chapter 2 chinensis and F. indicus
Page 149 and 150: Chapter 2 monodon and Group III of
Page 151 and 152: Chapter 2 Tiger shrimp (P. monodon)
Page 153 and 154: Chapter 2 ALF-1 was a partial seque
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Chapter 2 As mentioned before, the
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Chapter 2 Munoz et al., 2004). The
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Table 2.1. Primers used for the stu
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Table 2.4. BLASTn analysis of ALF-2
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Table 2.8. BLASTn analysis of Crust
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Table 2.12. BLASTn analysis of Pena
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Fig.2.5. Agarose gel electrophoreto
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Chapter 2 Fig.2.9. Multiple alignme
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Chapter 2 Fig. 2.12 A bootstrapped
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Chapter 2 Fig. 2.15. Multiple align
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Chapter 2 Fig.2.18. A bootstrapped
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Chapter 2 Fig.2.20. Signal peptide
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Chapter 2 Fig.2.24 Multiple alignme
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Chapter 2 LITOPENAEUS SP. FARFANTEP
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Chapter 2 Fig. 2.28. Nucleotide and
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Chapter 2 LITOPENAEUS SP. FENNEROPE
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Chapter 2 Fig.2.43 A bootstrapped n
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Chapter 2 LITOPENAEUS SP. FENNEROPE
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Chapter 2 Fig.2.51 Signal peptide a
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Chapter 2 FENNEROPENAEUS SP. FARFAN
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CHAPTER-3 Molecular Characterizatio
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Chapter 3 certainly help us to unra
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Chapter 3 3.3.1.1. Anti-lipopolysac
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Chapter 3 was predicted out to be 1
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Chapter 3 random coiled structure t
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3.3.1.3.5. Phylogenetic analysis of
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Chapter 3 case has been reported in
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Chapter 3 Multiple alignments were
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Chapter 3 negative bacteria. In shr
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Chapter 3 indicated a random coiled
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Chapter 3 horseshoe crab big defens
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Table 3.4. BLASTn analysis of ALF-2
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Table.3.8. BLASTn analysis of Fi-pe
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Chapter 3 Fig.3.2. Nucleotide and a
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Chapter 3 Fig.3.5. Multiple alignme
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Chapter 3 Fig.3.8. Nucleotide and a
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Chapter 3 Fig.3.12. Multiple alignm
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Chapter 3 Fig.3.14. A bootstrapped
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SHRIMPS KIND CRAB LOBSTERS CRABS Ch
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Chapter 3 Fig. 3.28. Multiple align
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PENAEIDIN-2 Chapter 3 PENAEIDIN- 3
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Fig.3.31. Nucleotide and amino acid
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Chapter 3 Fig.3.37 Nucleotide and a
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4.1. Introduction Chapter 4 The aqu
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Chapter 4 appearance and have major
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Chapter 4 the tissues has recently
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Chapter 4 with the ability of shrim
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Chapter 4 with a low dose of WSSV b
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Chapter 4 molecules they are likely
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Chapter 4 for understanding gene ex
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Chapter 4 4.3.2. Expression profile
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Expression profile of endonuclease
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Chapter 4 bacterial and fungal infe
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Chapter 4 measuring TSV and YHV loa
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Chapter 4 Of particular interest he
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Chapter 4 large distribution and ab
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Chapter 4 WSSV genes viz. endonucle
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Table 4.2. Primers used for the stu
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(A) (B) B 28 1 2 3 4 5 6 7 8 9 10 C
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(A) (B) B 28 1 2 3 4 5 6 7 8 9 10 C
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(A) (B) B 28 1 2 3 4 5 6 7 8 9 10 C
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(A) (B) B 28 1 2 3 4 5 6 7 8 9 10 C
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(A) (B) B 28 1 2 3 4 5 6 7 8 9 10 F
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(A) (B) B 28 1 2 3 4 5 6 7 8 9 10 C
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(A) (B) B 28 1 2 3 4 5 6 7 8 9 10 C
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(A) (B) B 28 1 2 3 4 5 6 7 8 9 10 C
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CHAPTER-5 Expression Profile of Ant
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Chapter 5 1994). The emergence of b
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Chapter 5 (Bovill et al., 2001). In
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5.2.2. Test diets Chapter 5 Four ex
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5.2.2.4. Preparation of Glucan inco
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Chapter 5 genes (latency related ge
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Chapter 5 On WSSV challenge, crusti
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Chapter 5 5.3.4. Expression profile
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5.3.4.5. Expression profile of pena
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Chapter 5 must firstly rest on a so
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Chapter 5 For the present study two
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Chapter 5 ameobocytes of two marine
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Chapter 5 variation in expression o
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Chapter 5 It has been previously sh
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Chapter 5 manifested in terms of gr
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(A) (B) (C) C CHY CSY CHG CSG C CHY
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(A) (B) -VE CTRL +VE CTRL CHG CSG C
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(A) PRE-CHALLENGE (B) POST-CHALLENG
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(A) PRE-CHALLENGE (B) (C) (D) CONTR
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(C) (D) (A) PRE-CHALLENGE (B) CONTR
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(A) (B) G M HP HR I Chapter 5 Fig.
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Chapter 5 Fig. 5.26. Post challenge
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6.1. Introduction Chapter 6 Prophyl
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Chapter 6 production of inhibitory
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6.2. Materials and methods 6.2.1. E
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Chapter 6 tissue cDNA was performed
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Chapter 6 gene was supported by Bac
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Chapter 6 treated group of shrimps.
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Chapter 6 the gene was found to be
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Chapter 6 found to support minimum
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Chapter 6 is induced upon bacterial
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Chapter 6 all the target genes, exc
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Chapter 6 Detailed tissue-wise anal
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Chapter 6 Gills and intestine was f
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(A) (B) Fig. 6.1. Experimental diet
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(A) (B) (C) Fig. 6.3. Expression pr
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(A) (B) (C) C B M BM C B M BM Fig.
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(A) (B) (C) Fig. 6.7. Expression pr
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(A) (B) (C) Chapter 6 Fig. 6.9. Exp
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(A) (B) -VE CTRL +VE CTRL B M BM Ch
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(A) (C) (D) PRE-CHALLENGE POST-CHAL
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(A) (B) G M HP HR I Chapter 6 Fig.
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Chapter 6 Fig. 6.27. Post challenge
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7.1. Summary Chapter 7 Tropical shr
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Salient findings Chapter 7 � From
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Chapter 7 � Tissue-wise expressio
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Chapter 7 application in shrimp cul
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References Aboudy, Y., Mendelson, E
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References Anggraeni, M.S., Owens,
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References Bals, R., Wang, X., Zasl
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References derived from the N-termi
Page 427 and 428:
References Breukink, E., de Kruijff
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References Burgents, J.E., Burnett,
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References 1,3-β-D-glucan-binding
Page 433 and 434:
References Chen, J.Y., Chuang, H.,
Page 435 and 436:
References Cole, A.M., Hong, T., Bo
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References Dathe, M., Wieprecht, T.
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References Diamond, G., Zasloff, M.
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References Faber, C., Stallmann, H.
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References Flint, S.J., Enquist, L.
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References Gennaro, R., Zanetti, M.
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References Gudmundsson, G.H., Lidho
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References Harwig, S.S., Swiderek,
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References Hirakura, Y., Kobayashi,
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References Huang, C.C., Song, Y.L.
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References Itami, T., Takahashi, Y.
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References Jiravanichpaisal, P. Whi
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References Kang, J.H., Shin, S.Y.,
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References Kono, T., Savan, R., Sak
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References rich peptide derived fro
Page 465 and 466:
References Li, L., Wang, J.X., Zhao
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References Liu, C.H., Cheng, W., Ku
Page 469 and 470:
References Lorenzon, S., de Guarrin
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References Marone, M., Mozzetti, S.
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References Medvinsky, A., Dzierzak,
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References Moriarty, D.J.W. 1996. M
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References antimicrobial peptide fr
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References Otta, S.K., Karunasagar,
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References simplex virus has heptad
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References infected shrimp. Thesis
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References Litopenaeus vannamei cha
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References Roth, B.L., Poot, M., Yu
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References Sathish, S., Musthaq, S.
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References a proline-arginine-rich
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References Smith, V.J., Fernandes,
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References Song, Y.L., Cheng, W., W
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References experimental system. In:
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References the black tiger shrimp P
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References Tapay, L.M., Cesar, E.,
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References Touhy, K.M., Probert, H.
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References van Hulten, M.C., Reijns
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References Yodmuang, S., Tirasophon
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References Zhan, W.B., Wang, Y.H. 1
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Penaeus monodon anti-lipopolysaccha
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Penaeus monodon crustin-like antimi
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Penaeus monodon crustin-like antimi
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Penaeus monodon penaeidin-like anti
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Penaeus monodon elongation factor m
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Fenneropenaeus indicus anti-lipopol
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Fenneropenaeus indicus penaeidin-li
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Fenneropenaeus indicus beta-actin m
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PUBLICATIONS
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Short sequence report Molecular cha
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Fig. 2. Multiple alignment of nucle
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220 The phylogenetic relationships
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Table 1 Rearing conditions and wate
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5 ′ cttgtggttgacaatggctccg3
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Expression of WSSV genes in the hae
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Fig. 4. Expression profile of crust
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S.P. Antony et al. / Immunobiology
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