A novel single-domain peptide, anti-LPS factor from prawn: Synthesis of peptide, antimicrobial properties and complete molecular characterization

Arockiaraj, Jesu; Kumaresan, Venkatesh; Bhatt, Prasanth; Palanisamy, R.; Gnanam, Annie J.; Pasupuleti, Mukesh; Krishnaveni, M.; Chaurasia, Mukesh Kumar

doi:10.1016/j.peptides.2013.11.008

Cited by 28 publications

(15 citation statements)

References 55 publications

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“…b), anti‐lipopolysaccharide factor (Arockiaraj et al . ) and lectin (Arockiaraj et al . ) have been characterized from M. rosenbergii .…”

Section: Immune Systemmentioning

confidence: 99%

“…Arockiaraj et al . () have reported a 13.8 kDa ALF protein (HF568844) with an anti‐LPS domain from M. rosenbergii which is highly expressed in haemocytes and they have also identified a helical amphipathic antimicrobial peptide region with hydrophilic and hydrophobic face ( 54 TCQYSVNPKIKRFELYFKGRMWCP 77 ) from Mr ALF. The peptide showed a strong binding activity against LPS of Gram negative bacteria and also inhibited the activity of Vibrio harveyi (Gram‐negative) and Streptococcus iniae (Gram‐positive).…”

Section: Immune Systemmentioning

confidence: 99%

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Impacts of environmental and biological stressors on immune system ofMacrobrachium rosenbergii

Kumaresan

Palanisamy

Pasupuleti

et al. 2016

Reviews in Aquaculture

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Macrobrachium rosenbergii commonly called giant freshwater prawn is a widely farmed crustacean in freshwater. Similar to other aquatic organisms, their growth and well-being is influenced by various physical, chemical and biological factors. We discuss about the critical growth limiting factors as well as disease causing agents and the potential immune molecules of M. rosenbergii that are proved to involve in preventing and/or responding to those limiting factors.

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“…b), anti‐lipopolysaccharide factor (Arockiaraj et al . ) and lectin (Arockiaraj et al . ) have been characterized from M. rosenbergii .…”

Section: Immune Systemmentioning

confidence: 99%

Section: Immune Systemmentioning

confidence: 99%

Impacts of environmental and biological stressors on immune system ofMacrobrachium rosenbergii

Kumaresan

Palanisamy

Pasupuleti

et al. 2016

Reviews in Aquaculture

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“…rosenbergii were injected with crude viral sample [white spot syndrome baculovirus (WSBV) and M. rosenbergii nodovirus (MrNV)] and bacteria (A. hydrophila and V. harveyi) (Arockiaraj et al 2013d). Viral-infected prawn tail tissue was homogenized in sterile 2% NaCl solution and injected to the prawn as reported in our earlier study (Arockiaraj et al 2014). Tissue homogenate prepared from healthy tail muscle served as control.…”

Section: Pathogen Injection and Sample Collectionmentioning

confidence: 99%

“…The predicted AMPs from MrH4 protein sequence were synthesized using solid-phase peptide synthesis technology as reported in our earlier study (Arockiaraj et al 2014). The synthesized peptides were further purified using reversed-phase HPLC (Hitachi Chromaster) and their homogeneity evaluated by HPLC analytical column.…”

Section: Synthesis Of N and C Terminal Peptides From Mrh4 Proteinmentioning

confidence: 99%

A prawn core histone 4: Derivation of N- and C-terminal peptides and their antimicrobial properties, molecular characterization and mRNA transcription

Chaurasia

Palanisamy

Bhatt

et al. 2015

Microbiological Research

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This study investigates the complete molecular characterization including bioinformatics characterization, gene expression, synthesis of N and C terminal peptides and their antimicrobial activity of the core histone 4 (H4) from freshwater giant prawn Macrobrachium rosenbergii (Mr). A cDNA encoding MrH4 was identified from the constructed cDNA library of M. rosenbergii during screening and the sequence was obtained using internal sequencing primers. The MrH4 coding region possesses a polypeptide of 103 amino acids with a calculated molecular weight of 11kDa and an isoelectric point of 11.5. The bioinformatics analysis showed that the MrH4 polypeptide contains a H4 signature at (15)GAKRH(19). Multiple sequence alignment of MrH4 showed that the N-terminal (21-42) and C-terminal (87-101) antimicrobial peptide regions and the pentapeptide or H4 signature (15-19) are highly conserved including in humans. The phylogenetic tree formed two separate clades of vertebrate and invertebrate H4, wherein MrH4 was located within the arthropod monophyletic clade of invertebrate H4 groups. Three-dimensional model of MrH4 was established using I-TASSER program and the model was validated using Ramachandran plot analysis. Schiffer-Edmundson helical wheel modeling was used to predict the helix propensity of N (21-42) and C (87-101) terminal derived Mr peptides. The highest gene expression was observed in gills and is induced by viral [white spot syndrome baculovirus (WSBV) and M. rosenbergii nodovirus (MrNV)] and bacterial (Aeromonas hydrophila and Vibrio harveyi) infections. The N and C terminal peptides were synthesized and their antimicrobial and hemolytic properties were examined. Both peptides showed activity against the tested Gram negative and Gram positive bacteria; however, the highest activity was noticed against Gram negative bacteria. Among the two peptides used in this study, C-terminal peptide yielded better results than the N-terminal peptide. Therefore, C terminal peptide can be recommended for the development of an antimicrobial agent.

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“…Functional characterization of ALFs has been conducted by chemically synthesizing the LPS domain region, [16][17][18][19][20][21][22] and by recombinant expression of mature peptides. 9,13,[23][24][25][26][27][28] Biological activity reported so far for ALFs include antibacterial, 6,9,20 antifungal, 6,27 antiviral, 29,30 immunomodulatory, 31 antitumor, 32 anti-inflammatory, and antiprotozoal activity.…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization and phylogenetic analysis of an anti-lipopolysaccharide factor from the crucifix crab, Charybdis feriatus

Sruthy¹,

Nair²,

Cubelio³

et al. 2015

OAAP

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Antimicrobial peptides are small cationic, gene-encoded, amphipathic, host defense peptides with a ubiquitous distribution in all living kingdoms. They are ,10 kDa in size, with 15-100 amino acids having a net positive charge of +2 to +9. Anti-lipopolysaccharide factor (ALF) is a cationic antimicrobial peptide which constitutes one of the key effector molecules in the innate immune system of crustaceans, and is capable of binding and neutralizing lipopolysaccharides. In the present study, an ALF homolog (Charybdis feriatus [Cf]-ALF1)-encoding cDNA sequence from the hemocytes of the crucifix crab, C. feriatus, was cloned, identified, and characterized. The deduced peptide of Cf-ALF1 encoded for a 123 amino acid peptide with a 97 residue mature peptide (11.16 kDa) that had a net charge of +10. Two conserved cysteine residues and a putative lipopolysaccharide binding domain were observed in the Cf-ALF1 mature peptide. BLAST analysis of Cf-ALF1 nucleotides showed a 99% similarity to Scylla serrata. The spatial structure of Cf-ALF1 was composed of three α-helices packed against a four-strand β-sheet. Two of these helices were linked by a disulfide bond to form an amphipathic loop similar to the structure of anti-lipopolysaccharide factor isoform 3 from Penaeus monodon (ALF-Pm3). All these features suggest that Cf-ALF1 could play a significant role in the innate immune defense mechanism of C. feriatus.

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A novel single-domain peptide, anti-LPS factor from prawn: Synthesis of peptide, antimicrobial properties and complete molecular characterization

Cited by 28 publications

References 55 publications

Impacts of environmental and biological stressors on immune system ofMacrobrachium rosenbergii

Impacts of environmental and biological stressors on immune system ofMacrobrachium rosenbergii

A prawn core histone 4: Derivation of N- and C-terminal peptides and their antimicrobial properties, molecular characterization and mRNA transcription

Molecular characterization and phylogenetic analysis of an anti-lipopolysaccharide factor from the crucifix crab, Charybdis feriatus

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