The amino acid sequences of jacalin and the <i>Maclura pomifera</i> agglutinin

Young, N. Martin; Johnston, Rosemary A.Z.; Watson, David

doi:10.1016/0014-5793(91)80518-8

Cited by 58 publications

(36 citation statements)

References 16 publications

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“…The sequence of the 250 amino acid polypeptide is identical to the recently published, conventionally derived, sequence of PNA [10], except for 14 additional amino acids at the C-terminal end. Recent analysis of the molecular size of mature PNA by mass spectrometry (N.M. Young, private communication) revealed that it consists of a major constituent of 236 amino acids (mol.…”

Section: Prepna-cdna Sequencingmentioning

confidence: 81%

“…The hemagglutination studies prove that rPNA is functionally equivalent to native PNA. A single N-terminal sequence, Ala.Glu-Thr-Val-SerPhe-Asn-Phe-Asn-Ser-Phe-Ser, was found in rPNA, identical to that of the native lectin [10].…”

Section: 3mentioning

confidence: 81%

“…This specificity allows for the use of PNA to detect the T-antigen on erythrocytes [1], and to separate mature and immature thymocytes of mouse [7] and man [8]. A partial sequence of PNA has been reported previously [9] and, while this work was being completed, a seque.nee of 236 amino acids of the leetin has been established by conventional techniques [10]. As expected, it shows extensive homology with the sequences of other legume lectins.…”

Section: Introductionmentioning

confidence: 87%

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Cloning, sequence analysis and expression in Escherichia coli of the cDNA encoding a precursor of peanut agglutinin

et al. 1992

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The eDNA coding for pro-peanut agglutinin (PNA) was isolated from a bacterial expression library, It codes for a polypeptide of 273 amino acids composed of a hydrophobie signal peptide of 23 amino acids and a mature protein of 250 amino acids, The sequence of the latter is identi~l to that of native PNA, determined very recently by conventional methods, e~cept that it contains 14 additional amino acids at the C-terminus. Bacterial cells harboring a plasmid with the prePNA--cDNA, produced two PNA cross-reacting proteins: one migrated on SDS-PAGE identically with the native lectin (apparent tool, wt. 31 kDa); the other, at 35 kDa. was a fl-galactosidase pre.PNA fusion protein, The former protein poss~sed an N-terminal sequence identical to that of the mature, native FNA, suggesting that it was processed from the 35 kDa prePNA precursor. Only the 31 kDa protein was exported into the bacterial perilalasmie space, and had the ability to bind to galactose-Sepharos¢, The isolated progcsz,:s~ protein had the same hemagglutinating activity as the native iectin, when assayed with sialidase-treated human erythro~ytcs. Like the native leetin, it did not agglutinate the untreated cells, was not inhibited by N.acetylgalactosamine, and was inhibited by Galfll ~3GalNAc 30-times more strongly than by ~.alactose, In this paper we report the isolation and characterisation of a eDNA encoding prePNA and the e~;pression of the recombinant active lectin in Escherichia coil, demonstrating that the precursor is processed by the bacteria and that only the processed form binds carbohydrate. Our results provide a basis for studies of the Abbre~,iations: PBS, phosphate.buffered saline; PNA, peanut a~gluti-nin; pPNAT, Bluescript plasmid containing prePNA.cDNA from clone C7; rPNA, recombinant PNA.

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Section: Prepna-cdna Sequencingmentioning

confidence: 81%

Section: 3mentioning

confidence: 81%

Section: Introductionmentioning

confidence: 87%

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Cloning, sequence analysis and expression in Escherichia coli of the cDNA encoding a precursor of peanut agglutinin

et al. 1992

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“…Heterogeneity (isolectins and N-glycosylation) is widely known in JRLs. [5][6][7]48) Sugar content of TAA-G was estimated to be less than 2.5 µg/mg protein (0.24 sugar residue/mole protein) by phenol-sulfuric method. Furthermore, no Asn-X-Ser (Thr) sequence was found in TAA-G.…”

Section: Discussionmentioning

confidence: 99%

“…4) gJRLs are synthesized as preproproteins, which undergo co-and post-translational processing, and built up of cleaved protomers, short β-chain and long α-chain. [5][6][7] On the contrary, mJRLs are not cleaved and have a single polypeptide chains. gJRLs are produced by the cleavage of a loop in mJRL homologs, resulting that gJRLs show the preference to galactose and N-acetyl galactosamine.…”

mentioning

confidence: 99%

Two jacalin-related lectins from seeds of the African breadfruit (Treculia africana L.)

Shimokawa

Nsimba-Lubaki

Hayashi

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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Two jacalin-related lectins (JRLs) were purified by mannose-agarose and melibiose-agarose from seeds of Treculia africana. One is galactose-recognizing JRL (gJRL), named T. africana agglutinin-G (TAA-G), and another one is mannose-recognizing JRL (mJRL), TAA-M. The yields of the two lectins from the seed flour were approximately 7.0 mg/g for gJRL and 7.2 mg/g for mJRL. The primary structure of TAA-G was determined by protein sequencing of lysyl endopeptic peptides and chymotryptic peptides. The sequence identity of TAA-G to other gJRLs was around 70%. Two-residue insertion was found around the sugar-binding sites, compared with the sequences of other gJRLs. Crystallographic studies on other gJRLs have shown that the primary sugar-binding site of gJRLs can accommodate Gal, GalNAc, and GalNAc residue of T-antigen (Galβ1-3GalNAcα-). However, hemagglutination inhibition and glycan array showed that TAA-G did not recognize GalNAc itself and T-antigen. TAA-G preferred melibiose and core 3 O-glycan.

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Identification of N‐Acetylgalactosamine in Carbohydrates of Xenopus laevis Testis

Valbuena

Alonso

Díaz‐Flores

et al. 2010

The Anatomical Record

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Identification of glycans in amphibian testis has shown the existence of N-acetylgalactosamine (GalNAc)-containing carbohydrates. Labeling of the sperm acrosome with GalNAc-binding lectins has allowed the identification of GalNAc-containing glycans in this organelle. Futhermore, this specific labeling of the acrosome has allowed the study of acrosomal biogenesis by lectin histochemistry. However, the testis of Xenopus laevis has never been analyzed by lectin histochemistry to locate GalNAc-containing glycoconjugates. The aim of this work was to elucidate the expression of GalNAc in glycoconjugates of Xenopus testis using five specific lectins. The results showed that most of the lectins labeled the interstitium with variable intensity. However, labeling of the different spermatogenetic germ cell types showed different labeling patterns. Some lectins produced weak or very weak staining in germ cells, for example, horse gram Dolichos biflorus agglutinin, which labeled most of the germ cell types, and lima bean Phaseolus lunatus agglutinin, which weakly labeled only spermatogonia, but did not stain other germ cells. By contrast, Maclura pomifera lectin (MPL) moderately labeled all germ cell types, except mature sperm. Labeling with other lectins was seen only at later stages, suggesting variations involved in the spermatogenetic development. Thus, snail Helix pomatia agglutinin labeled spermatids, but neither spermatogonia nor spermatocytes, while soybean Glycine max agglutinin (SBA) labeled from preleptotene spermatocytes to later stages. The periphery of the acrosome was labeled with MPL and SBA, but no specific labeling of the acrosomal content was seen with any lectin. Thus, the GalNAc-binding lectins that have been used as acrosomal markers in some amphibians cannot be used in Xenopus testis, suggesting that acrosomal glycoconjugates in amphibians are species specific.

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The amino acid sequences of jacalin and the Maclura pomifera agglutinin

Cited by 58 publications

References 16 publications

Cloning, sequence analysis and expression in Escherichia coli of the cDNA encoding a precursor of peanut agglutinin

Cloning, sequence analysis and expression in Escherichia coli of the cDNA encoding a precursor of peanut agglutinin

Two jacalin-related lectins from seeds of the African breadfruit (Treculia africana L.)

Identification of N‐Acetylgalactosamine in Carbohydrates of Xenopus laevis Testis

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