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amino acid sequences of crustins also showed that the deduced amino acids of Fi-crustin shared relatively high identities with those of F. chinensis and P. monodon. Multiple alignment of the nucleotide sequences of Fi-crustin and other shrimp crustins showed high similarity in the signal peptide region, major gaps could be observed in the ensuing region. The 58e70th nucleotide sequences were found to be absent in the Fi-crustin when compared to P. monodon crustin sequence. A similar gap could be observed for the F. chinensis crustins between the 64e70th position. Similarly, another missing S.P. Antony et al. / Fish & Shellfish Immunology 28 (2010) 216e220 219 Fig. 3. A bootstrapped neighbor-joining tree obtained using MEGA version 4.0 illustrating relationships between the deduced amino acid sequence of the Fenneropenaeus indicus crustin-like AMP, Fi-crustin (GQ469987) with other crustins of decapod crustaceans (Litopenaeus vannamei AF430071, L. vannamei AF430074, L. vannamei AY488497, L. vannamei AY488492, Litopenaeus setiferus AF430078, Farfantepenaeus paulensis EF182747, L. vannamei AY488493, L. vannamei AF430073, L. vannamei AY486426, L. vannamei AF430072, Farfantepenaeus subtilis EF450744, Litopenaeus schmitti EF182748, L. vannamei AY488496, L. vannamei AY488495, L. vannamei AF430075, L. vannamei AF430076, L. vannamei AY488494, Farfantepenaeus brasiliensis EF601055, L. schmitti EF601056, Fenneropenaeus chinensis AY871268, Marsupenaeus japonicus AB121740, Penaeus monodon FJ539174, P. monodon EF654659, P. monodon FJ539178, P. monodon EF654658, P. monodon GQ334395, P. monodon GQ334396, P. monodon FJ539175, P. monodon FJ539177, F. chinensis DQ097704, F. chinensis DQ097703, Paralithodes camtschaticus EU921643, Pacifastacus leniusculus 1 EF523614, Homarus americanus EF193003, Homarus gammarus AJ786653, Scylla paramamosain EU161287, Hyas araneus EU921642, Hyas araneus EU921641). Values at the node indicate the percentage of times that the particular node occurred in 1000 trees generated by bootstrapping the original deduced protein sequences. sequence region could be observed for Fi-crustin between the 88e98th position that matches with a similar gap for the F. chinensis crustins at the 88e93rd position, when compared to P. monodon. Great variation between the sequences of P. monodon and Fenneropenaeus sp. could be observed at the 122nde144th position. Other major missing sequences of the Fi-crustins were found at 182e202nd and also between 211th and 216th position. F. chinensis showed a major gap for the nucleotide sequences at 262e352nd position whereas P. monodon and Fi-crustin did not.
220 The phylogenetic relationships between Fi-crustin and other crustins with WAP domain are shown in Fig. 3. The tree topologies revealed the relationships of Fi-crustin with other invertebrate crustin-like peptides. The molecular phylogenetic tree based on amino acid sequences suggests that all the crustin members possess the same ancestral origin, which has subsequently diverged at different phases of evolution. Out of all the species, crustins of prawns are found to be evolutionarily distantly related to crustins of other decapod species. The tree could be broadly classified into three major groups, one major group (Group I) which included the crustins of prawns; another (Group II) with that of king crab/ crayfish crustins and Group III containing the lobster/crab crustins. The bootstrap distance tree calculated for the crustin sequences clearly indicate that the Fi-crustin possessed great similarity to crustins isolated from F. chinensis and P. monodon. Great variability could also be noticed in the crustin sequences of various decapods. This is the first report of an antimicrobial peptide from Indian white prawn, F. indicus .The reported AMP belonged to the class of crustins with its characteristic WAP domain and showed 91% similarity to F. chinensis crustins. The phylogenetic tree analysis showed that the crustins diverged from an ancestral sequence to three major groups i.e. Group 1 with prawns, Group II with Crayfishes/King crabs and Group III with Lobsters/Crabs. Under prawn e crustins, three sub groups were noticed 1) L. vannamei 2) P. monodon and 3) Fenneropenaeus sp. The wide distribution of crustins in crustaceans indicates the importance of these antimicrobial peptides in the innate immune system. Acknowledgments The authors are grateful to the Ministry of Earth Sciences (MoES), Govt. of India for the research grant (MoES/10-MLR/2/ 2007) with which the work was carried out. The first author gratefully acknowledges KSCSTE (Kerala State Council for Science, Technology and Environment) for the award of the fellowship. References [1] Boman HG. Antibacterial peptides: basic facts and emerging concepts. J Intern Med 2003;254:197e215. [2] Dimarcq JL, Bulet P, Hetru C, Hoffmann J. Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers 1998;47:465e77. [3] Bulet P, Hetru C, Dimarq JL, Hoffman D. Antimicrobial peptides in insects; structure and function. Dev Comp Immunol 1999;23:329e44. [4] Destoumieux D, Munoz M, Bulet P, Bachere E. Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda). Cell Mol Life Sci 2000;57:1260e71. [5] Cuthbertson BJ, Deterding LJ, Williams JG, Tomer KB, Etienne K, Blackshear PJ, et al. GrossPS. Diversity in penaeidin antimicrobial peptide form and function. Dev Comp Immunol 2008;32:167e81. [6] Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415:389e95. 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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
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1.7 Antimicrobial Peptides (AMPs) 1
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Chapter 1 the response is very fast
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Chapter 1 Hirsch, 1947). While they
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Chapter 1 AMPs to various degrees u
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1.7.5 Biological activity Chapter 1
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Chapter 1 including the microbes as
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Tachyplesin I Chapter 1 Crustacea P
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Anionic and cationic peptides that
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Anionic and Cationic AMPs with cyst
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Chapter 1 Fig. 1.7. Structural clas
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Chapter 1 Group III: Linear peptide
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Chapter 1 through regular processes
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Chapter 1 ultimately signal to tran
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Chapter 1 divalent polyanionic cati
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Chapter 1 type of transmembrane por
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Chapter 1 other intracellular targe
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Chapter 1 Apidaecin, a short, proli
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Chapter 1 Hultmark, 1987; Gennaro a
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Chapter 1 quite opposite characteri
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Chapter 1 depletion of mitochondria
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Chapter 1 conformations adopted by
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Chapter 1 receptor may be a potenti
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Chapter 1 exposure to their targets
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Chapter 1 generating a rich spectru
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Chapter 1 by enkelytin (Goumon et a
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Lactoferricin Cow Mastitis control
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Chapter 1 trial, in which peptide T
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Chapter 1 a too limited spectrum to
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Chapter 1 number of research groups
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CHAPTER-2 Molecular Characterizatio
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Chapter 2 interaction with negative
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Chapter 2 inhibit the endotoxin or
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Chapter 2 structure be modified to
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Chapter 2 and the region might be l
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Chapter 2 been made of the spectra
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Chapter 2 their discovery and initi
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Chapter 2 terminal pyroglutamic aci
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Chapter 2 One can assume that the p
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Chapter 2 by degranulation into the
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2.2. Materials and Methods 2.2.1. E
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Chapter 2 washed by adding 1 ml 75
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Chapter 2 entry of recombinant DNA
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Chapter 2 and the deduced amino aci
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Chapter 2 Fenneropenaeus, Litopenae
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2.3.1.3. Crustin-1 (GQ334395) Chapt
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2.3.1.3.5. Phylogenetic analysis of
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Chapter 2 sequence also showed high
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Chapter 2 chinensis and F. indicus
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Chapter 2 monodon and Group III of
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Chapter 2 Tiger shrimp (P. monodon)
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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
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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
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References Chen, J.Y., Chuang, H.,
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References Cole, A.M., Hong, T., Bo
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References Dathe, M., Wieprecht, T.
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References Lorenzon, S., de Guarrin
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Page 507 and 508: References Vives, R.R., Imberty, A.
Page 509 and 510: References Wang, Y.C., Chang, P.S.,
Page 511 and 512: References Williams, M.J., Rodrigue
Page 513 and 514: References Wu, W., Zong, R., Xu, J.
Page 515 and 516: References Yodmuang, S., Tirasophon
Page 517 and 518: References Zhan, W.B., Wang, Y.H. 1
Page 519 and 520: Penaeus monodon anti-lipopolysaccha
Page 521 and 522: Penaeus monodon crustin-like antimi
Page 523 and 524: Penaeus monodon crustin-like antimi
Page 525 and 526: Penaeus monodon penaeidin-like anti
Page 527 and 528: Penaeus monodon elongation factor m
Page 529 and 530: Fenneropenaeus indicus anti-lipopol
Page 531 and 532: Fenneropenaeus indicus penaeidin-li
Page 533 and 534: Fenneropenaeus indicus beta-actin m
Page 535 and 536: PUBLICATIONS
Page 537 and 538: Short sequence report Molecular cha
Page 539: Fig. 2. Multiple alignment of nucle
Page 543 and 544: Table 1 Rearing conditions and wate
Page 545 and 546: 5 ′ cttgtggttgacaatggctccg3
Page 547 and 548: Expression of WSSV genes in the hae
Page 549 and 550: Fig. 4. Expression profile of crust
Page 551 and 552: S.P. Antony et al. / Immunobiology
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Molecular Characterization and Gene Expression Profiling ... - CUSAT

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