Chemical characterization of the lectin from the freshwater prawn Macrobrachium rosenbergii (De Man) by MALDI-TOF

Zenteno, Roberto; Vázquez, Lorena; Sierra, Claudia; Pereyra, Ali; Slomianny, Marie Christine; Bouquelet, Stéphane; Zenteno, Edgar

doi:10.1016/s0305-0491(00)00260-1

Cited by 23 publications

(8 citation statements)

References 26 publications

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“…Its carbohydrate moiety was quite di¡erent form the CHA-I lectin consisting of xylose and fucose [1,16]. The active form of sialic acid-speci¢c lectin of the freshwater prawn Macrobrachium rosenbergii was a dimeric glycoprotein with 9.5 kDa per subunit [23], or the lectin of the Southeast Asian horseshoe crab Tachypleus gigas which had a molecular mass of 396 kDa and was composed of 13 identical subunits with a molecular mass of 31 kDa [19]. Bands were cut out, eluted by 0.2 ml 1% SDS solution and the absorbances at 592 nm were measured.…”

Section: Discussionmentioning

confidence: 99%

Chemical and physicochemical characterization of the sialic acid-specific lectin from Cepaea hortensis

Gerlach

2002

FEMS Microbiology Letters

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A sialic acid-specific lectin was isolated from the albumin glands of the garden snail Cepaea hortensis by affinity chromatography on fetuin-Sepharose following gel filtration on Superdex 200. The purified native lectin showed a molecular mass of about 95 kDa by gel filtration and 100 kDa by SDS electrophoresis. It was cleaved by boiling in buffer containing SDS in three serological identical bands corresponding to molecular masses of about 24, 20 and 16 kDa, respectively. From these three fragments, only the 24-and the 20-kDa bands were found to be glycosylated. Only the three sugars mannose, galactose and N-acetylglucosamine could be detected in a molar ratio of 3:8.6:2. The oligosaccharide moieties seem to be N-and partially O-glycosidic bound. Isoelectric focusing (IEF) of the purified lectin revealed a heterogeneous pattern with bands in the pH range of 4.3^5.0. Isolated bands of different isoelectric points showed in SDS electrophoresis the same three fragments with molecular masses of 24, 20 or 16 kDa. The heterogeneity of the lectin was revealed either by IEF or amino acid sequencing of internal tryptic peptides. ß

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Section: Discussionmentioning

confidence: 99%

Chemical and physicochemical characterization of the sialic acid-specific lectin from Cepaea hortensis

Gerlach

2002

FEMS Microbiology Letters

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“…LvCTL1 protein was not detected in the hemolymph of healthy (unchallenged) shrimps. After WSSV infection, a 24-kDa protein was detected in the hemolymph at 12 h postinfection, which was assumed to be the natural glycoprotein of LvCTL1, just like other shrimp lectin glycoproteins from Fenneropenaeus merguiensis, Penaeus monodon, and Macrobrachium rosenbergii (32,33,50). The concentration of LvCTL1 in hemolymph increased steadily up to 48 h postinfection (Fig.…”

Section: Comparison Of Lvctl1 With Other Shrimp C-type Lectinsmentioning

confidence: 99%

A Novel C-Type Lectin from the Shrimp Litopenaeus vannamei Possesses Anti-White Spot Syndrome Virus Activity

Zhao

Yin

et al. 2009

J Virol

199

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C-type lectins play key roles in pathogen recognition, innate immunity, and cell-cell interactions. Here, we report a new C-type lectin (C-type lectin 1) from the shrimp Litopenaeus vannamei (LvCTL1), which has activity against the white spot syndrome virus (WSSV). LvCTL1 is a 156-residue polypeptide containing a C-type carbohydrate recognition domain with an EPN (Glu 99 -Pro 100 -Asn 101 ) motif that has a predicted ligand binding specificity for mannose. Reverse transcription-PCR analysis revealed that LvCTL1 mRNA was specifically expressed in the hepatopancreas of L. vannamei. Recombinant LvCTL1 (rLvCTL1) had hemagglutinating activity and ligand binding specificity for mannose and glucose. rLvCTL1 also had a strong affinity for WSSV and interacted with several envelope proteins of WSSV. Furthermore, we showed that the binding of rLvCTL1 to WSSV could protect shrimps from viral infection and prolong the survival of shrimps against WSSV infection. Our results suggest that LvCTL1 is a mannose-binding C-type lectin that binds to envelope proteins of WSSV to exert its antiviral activity. To our knowledge, this is the first report of a shrimp C-type lectin that has direct anti-WSSV activity.

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“…Zenteno et al [49] reported MrL has homology with a M. rosenbergii's crustacean hyperglycemic hormone; Alpuche et al [17] indicated homology of two subunits of LsL with L. vannamei's hemocyanin; it is possible that the proteins in the crustacean could have the same phylogenetic origin. It is well established that all proteins present in organisms are derived from a limited set of archetypal proteins.…”

Section: Discussionmentioning

confidence: 97%

The Use of Monoclonal Antibodies Anti-Lectin from Freshwater PrawnMacrobrachium rosenbergii(DeMan, 1879) in the Recognition of Protein with Lectin Activity in Decapod's Hemolymph

Pereyra

Agundis

Barrera

et al. 2009

Preparative Biochemistry and Biotechnology

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We determined the cross-reactivity of a monoclonal antibody against the Macrobrachium rosenbergii lectin with proteins in the hemolymph from Procambarus clarkii (Pc), Procambarus americanus (Pa), Litopenaeus setiferus (Ls), and Pseudothelphusa americana (Psa). Crustaceans' hemolymph agglutinated erythrocytes from rat, mouse, guinea pig, and rabbit. Decapods' hemolymph hemagglutinating activity was inhibited by N-acetylated carbohydrates as well as by antibodies. Western blot assays indicated that the antibodies recognized two main proteins of 97.5 and 80.9 kDa in all hemolymphs studied; moreover, ELISA assays indicated that, in PSa, 7.2% of total proteins showed crossreactivity with antibodies in Pa, Pc, and Lc hemolymphs represented 4.2, 3.1%, and 2.5%, respectively. Our results suggested that antibodies recognize the lectin active site in the crustacean species tested; we propose the use of antibodies as an immunological marker for lectin identification and quantification among crustaceans.

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Chemical characterization of the lectin from the freshwater prawn Macrobrachium rosenbergii (De Man) by MALDI-TOF

Cited by 23 publications

References 26 publications

Chemical and physicochemical characterization of the sialic acid-specific lectin from Cepaea hortensis

Chemical and physicochemical characterization of the sialic acid-specific lectin from Cepaea hortensis

A Novel C-Type Lectin from the Shrimp Litopenaeus vannamei Possesses Anti-White Spot Syndrome Virus Activity

The Use of Monoclonal Antibodies Anti-Lectin from Freshwater PrawnMacrobrachium rosenbergii(DeMan, 1879) in the Recognition of Protein with Lectin Activity in Decapod's Hemolymph

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