Isolation and characterization of immunoglobulin of the Indian major carp, rohu [Labeo rohita (Ham.)]

Babu, P P Suresh; Shankar, K. M.; Honnananda, B.R.; Swamy, H.V. Vijaya Kumara; Shama, K. Prasanna; Suryanarayana, V.V.S.; Dechamma, H J

doi:10.1016/j.fsi.2008.01.013

Cited by 18 publications

(7 citation statements)

References 30 publications

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“…For S. kneri Garman, the cysteine residues that exist in its sIgM heavy chain have great importance to its polymer structure. Specifically, the cysteine residues situated in the CH4 region of the sIgM heavy chain explain the generation of dimerized or tetrameric structures of the two heavy chains, which is solid support for the hypothesis that the sIgM molecules of S. kneri Garman are tetrameric (Rathore et al, 2008; Suresh Babu et al, 2008).…”

Section: Discussionmentioning

confidence: 66%

Secretory immunoglobulin M (sIgM) heavy chain gene in Siniperca kneri Garman: Molecular characterization and expression analysis in response to Aeromonas hydrophila challenge

Liu

Yang

et al. 2021

Aquaculture Research

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Immunoglobulin M (IgM) is widely recognized as the major isotype of teleost immunoglobulins. Its role in protecting fish against a number of pathogens is critical. In the current study, the IgM heavy chain gene of Siniperca kneri Garman was cloned for the first time. Its IgM heavy chain cDNA is 1952 bp in length and encodes a polypeptide of 583 amino acid residues, which includes a signal peptide, a variable region (VH) and four constant regions (CH1, CH2, CH3 and CH4). This confirms the secretory pattern of IgM (sIgM). The sIgM amino acid sequence shares high identity with those of Siniperca chuatsi (88.57%), Lateolabrax japonicus (65.73%) and Latris lineata (64.92%). Analysis of phylogenetic trees shows that the sIgM of S. kneri Garman is clustered with perciformes fish homologues and constructed as one clade. QRT‐PCR analysis found the highest sIgM expression in the head kidney, with higher expressions in the spleen and liver than in the brain, intestine, mesonephros, gill, skin and heart. After Aeromonas hydrophila injection, the sIgM expression pattern was up‐regulated and peaks occurred in the head kidney, spleen, intestine and gill on days 5, 7 and 21 post‐challenge. Changes in the peak expression of sIgM compared to controls were most significant in the head kidney (38.59‐fold) and spleen (23.75‐fold), with smaller differences in the gill (9.54‐fold) and intestine (7.75‐fold). This suggests that it is possible that sIgM is of greater importance to systemic immunity than mucosal immunity. Its importance to the adaptive immune response is thereby confirmed.

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Section: Discussionmentioning

confidence: 66%

Secretory immunoglobulin M (sIgM) heavy chain gene in Siniperca kneri Garman: Molecular characterization and expression analysis in response to Aeromonas hydrophila challenge

Liu

Yang

et al. 2021

Aquaculture Research

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“…1). Previously, Suresh et al (2008) reported HC and LC of affinity purified rohu Ig as 85 kDa and 23 kDa bands, respectively. In agreement with our results, Bag et al (2009) reported HC and LC for catla, rohu and mrigal Ig to be 88 and 26 kDa respectively.…”

Section: Resultsmentioning

confidence: 97%

Production and characterisation of monoclonal antibodies against immunoglobulins of Cirrhinus mrigala (Hamilton 1822)

Mohanty¹,

Makesh²,

Rajendran³

et al. 2020

Indian J. Fish.

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Serum immunoglobulins (Ig) of mrigal Cirrhinus mrigala (Hamilton 1822) immunised with bovine serum albumin (BSA), were purified by affinity chromatography using BSA-CL agarose column. The purified mrigal Ig (m-Ig) was characterised under reducing condition by Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE) which revealed two bands of 85 and 26 kDa corresponding to heavy and light chain, respectively. Following fusion of splenocytes from Balb/c mice immunised with purified m-Ig with myeloma cells, three hybridomas showing reactivity with m-Ig were cloned by limiting dilution. The monoclonal antibodies (MAbs) generated by these clones were designated as 3B2-E12, 3B2-F9 and 4C3-B2 and characterised by western blotting and isotyping. Western blot analysis of the supernatant from the three clones with purified m-Ig indicated that, all the three MAbs were specific to heavy chain. Isotyping revealed that 3B2-E12 MAb was of IgG1 isotype whereas the other two MAbs were of IgG2a isotype. Cross reactivity of anti-mrigal Ig MAb (3B2-E12) was observed with serum Ig of Catla catla and Labeo rohita indicating semi-conserved nature of Ig in Indian major carps.

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“…Five mrigal fishes weighing about 500 g each, maintained in a 25 m [ 2 ] cement cistern at the freshwater fish farm of the College of Fisheries, Mangaluru, were injected intraperitoneally (ip) each with 1 mg bovine serum albumin (BSA, Merck, India) dissolved in 250 μ l of phosphate buffered saline (PBS, pH 7.4) emulsified with an equal volume of Freund's complete adjuvant (FCA). Similar doses of BSA emulsified with an equal volume of Freund's incomplete adjuvant (FIA) were given 15 and 22 days later.…”

Section: Methodsmentioning

confidence: 99%

“…Fish immunoglobulins share various characteristics with mammalian immunoglobulin; however, some differences exist; those partly arise from the process of evolution from common ancestors and partly reflect the effect of fish adaptation to a changed life environment. The fish immune system contains five types of immunoglobulins: IgM [ 1 ], IgD [ 2 – 4 ], IgZ [ 5 ], IgT [ 6 ], and IgH [ 7 ]. The major immunoglobulin of fish blood serum is tetrameric IgM-like molecule [ 7 ] consisting of eight light and eight heavy chains.…”

Section: Introductionmentioning

confidence: 99%

“…The major immunoglobulin of fish blood serum is tetrameric IgM-like molecule [ 7 ] consisting of eight light and eight heavy chains. The teleost fish IgM shares some structural and functional characteristics with mammalian IgM; hence, we understand the ability of various teleost fishes to produce heterogeneous mixtures of IgM polymers, monomers [ 2 , 8 , 9 ], and halfmer subunits [ 10 ].…”

Section: Introductionmentioning

confidence: 99%

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Isolation, Production, and Characterization of Serum Immunoglobulin M (IgM) of Indian Major Carp Cirrhinus mrigal (MRIGAL)

Khandige

Shankar

Babu

et al. 2022

Advances in Pharmacological and Pharmaceutical Sciences

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A method for the isolation of immunoglobulin M (IgM) in Indian major carp Cirrhinus mrigal (mrigal) serum to produce polyclonal antibodies is described in the present study. The purified immunoglobulins (IgM) were isolated from the serum of mrigal (Cirrhinus mrigal) by the bovine serum albumin (BSA)-CL affinity column purification method, and the IgM was used to produce a polyclonal rabbit anti-mrigal IgM antiserum. The IgM preparations were employed in the characterization of mrigal serum immunoglobulin. Reduced mrigal IgM on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was shown to consist of two subunits, compatible with heavy and light chains. A single heavy chain at approximately 90 kDa and variant of light chain 30 kDa were found. The dominant form of nonreduced IgM had a MW of approximately 900 kDa, suggesting a tetrameric structure based on estimated molecular weights, the relative protein content, and the reactivity with anti-mrigal IgM antisera, was obtained. The antisera were characterized as to specificity and reactivity by means of the enzyme linked immuno-sorbent assay (ELISA) and western blotting method. The information on the structure and character of immunoglobulin of fishes is essential in health management. The study described here investigates the possibility of using the serological techniques to assess the reactivity of antibody with the anti-mrigal IgM antisera.

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Isolation and characterization of immunoglobulin of the Indian major carp, rohu [Labeo rohita (Ham.)]

Cited by 18 publications

References 30 publications

Secretory immunoglobulin M (sIgM) heavy chain gene in Siniperca kneri Garman: Molecular characterization and expression analysis in response to Aeromonas hydrophila challenge

Secretory immunoglobulin M (sIgM) heavy chain gene in Siniperca kneri Garman: Molecular characterization and expression analysis in response to Aeromonas hydrophila challenge

Production and characterisation of monoclonal antibodies against immunoglobulins of Cirrhinus mrigala (Hamilton 1822)

Isolation, Production, and Characterization of Serum Immunoglobulin M (IgM) of Indian Major Carp Cirrhinus mrigal (MRIGAL)

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