Identification of <i>N</i>‐acetylglucosamine binding residues in <i>Griffonia simplicifolia</i> lectin II

Zhu, Keyan; Bressan, Ray A.; Hasegawa, Paul M.; Murdock, Larry L.

doi:10.1016/0014-5793(96)00671-0

Cited by 32 publications

(24 citation statements)

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“…3D and E) (59). Pretreatment of Plasmodium glycoproteins with peptide:N-glycanaseF (PNGaseF) substantially decreases the binding of the GSL-II.…”

Section: Resultsmentioning

confidence: 99%

“…3, 4, and 6; see Fig. S2 and S3 in the supplemental material) (59). As GSL-II, like WGA-1 and other GlcNAc-binding lectins, may have a weaker affinity for a single GlcNAc rather than GlcNAc polymers, we may have failed to (secreted)..................................................................... c Relative protein abundance was estimated from the area/height results using SEAQUEST.…”

Section: Discussionmentioning

confidence: 99%

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Suggestive Evidence for Darwinian Selection against Asparagine-Linked Glycans of Plasmodium falciparum and Toxoplasma gondii

et al. 2010

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We are interested in asparagine-linked glycans (N-glycans) of Plasmodium falciparum and Toxoplasma gondii, because their N-glycan structures have been controversial and because we hypothesize that there might be selection against N-glycans in nucleus-encoded proteins that must pass through the endoplasmic reticulum (ER) prior to threading into the apicoplast. In support of our hypothesis, we observed the following. First, in protists with apicoplasts, there is extensive secondary loss of Alg enzymes that make lipid-linked precursors to N-glycans. Theileria makes no N-glycans, and Plasmodium makes a severely truncated N-glycan precursor composed of one or two GlcNAc residues. Second, secreted proteins of Toxoplasma, which uses its own 10-sugar precursor (Glc 3 Man 5 GlcNAc 2 ) and the host 14-sugar precursor (Glc 3 Man 9 GlcNAc 2 ) to make N-glycans, have very few sites for N glycosylation, and there is additional selection against N-glycan sites in its apicoplasttargeted proteins. Third, while the GlcNAc-binding Griffonia simplicifolia lectin II labels ER, rhoptries, and surface of plasmodia, there is no apicoplast labeling. Similarly, the antiretroviral lectin cyanovirin-N, which binds to N-glycans of Toxoplasma, labels ER and rhoptries, but there is no apicoplast labeling. We conclude that possible selection against N-glycans in protists with apicoplasts occurs by eliminating N-glycans (Theileria), reducing their length (Plasmodium), or reducing the number of N-glycan sites (Toxoplasma). In addition, occupation of N-glycan sites is markedly reduced in apicoplast proteins versus some secretory proteins in both Plasmodium and Toxoplasma.

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“…3D and E) (59). Pretreatment of Plasmodium glycoproteins with peptide:N-glycanaseF (PNGaseF) substantially decreases the binding of the GSL-II.…”

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Suggestive Evidence for Darwinian Selection against Asparagine-Linked Glycans of Plasmodium falciparum and Toxoplasma gondii

et al. 2010

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“…By this technique, several plant lectins, among them of pea (Stubbs et. al., 1986;and Van Eijsden et al, 1992), Erythrina corallodendron (Arango et al, 1993), peanut (Sharma and Surolia, 1994) and Griffonia simplicifolia (Zhu et al, 1996) have been expressed in Escherichia coli. Expression of plant lectins was also achieved in other systems, e.g.…”

Section: Isolate and Purification Of Lectinmentioning

confidence: 99%

Antimicrobial activity of lectins from Antimicrobial Activity of Lectins from Plants

Karnchanatat¹

2012

Antimicrobial Agents

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“…rGSII-and various site-specific mutagenized (D88N, Y134G, Y134D, Y134F, N136D, N136Q, and N196D) rGSII-encoding cDNAs in pET9c were obtained as described (33). The inserts were digested with NdeI and BamHI and ligated into pET28 vector.…”

Section: Methodsmentioning

confidence: 99%

“…Both leaf and seed GSII and bacterially expressed rGSII delayed significantly the development of C. maculatus (15). Site-directed mutagenesis was used to identify residues in rGSII essential for GlcNAc-binding activity (33). In the present study, we establish, through bioassays comparing rGSII and variant forms with neutral or GlcNAc-binding null mutations, that GlcNAc binding is required for insecticidal activity of rGSII against the cowpea bruchid.…”

mentioning

confidence: 96%

Carbohydrate binding and resistance to proteolysis control insecticidal activity of Griffonia simplicifolia lectin II

Zhu‐Salzman

Shade²,

Koiwa³

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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119

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Griffonia simplicifolia leaf lectin II (GSII), a plant defense protein against certain insects, consists of an N-acetylglucosamine (GlcNAc)-binding large subunit with a small subunit having sequence homology to class III chitinases. Much of the insecticidal activity of GSII is attributable to the large lectin subunit, because bacterially expressed recombinant large subunit (rGSII) inhibited growth and development of the cowpea bruchid, Callosobruchus maculatus (F). Site-specific mutations were introduced into rGSII to generate proteins with altered GlcNAc binding, and the different rGSII proteins were evaluated for insecticidal activity when added to the diet of the cowpea bruchid. At pH 5.5, close to the physiological pH of the cowpea bruchid midgut lumen, rGSII recombinant proteins were categorized as having high (rGSII, rGSII-Y134F, and rGSII-N196D mutant proteins), low (rGSII-N136D), or no (rGSII-D88N, rGSII-Y134G, rGSII-Y134D, and rGSII-N136Q) GlcNAc-binding activity. Insecticidal activity of the recombinant proteins correlated with their GlcNAc-binding activity. Furthermore, insecticidal activity correlated with the resistance to proteolytic degradation by cowpea bruchid midgut extracts and with GlcNAc-specific binding to the insect digestive tract. Together, these results establish that insecticidal activity of GSII is functionally linked to carbohydrate binding, presumably to the midgut epithelium or the peritrophic matrix, and to biochemical stability of the protein to digestive proteolysis.

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Identification of N‐acetylglucosamine binding residues in Griffonia simplicifolia lectin II

Cited by 32 publications

References 24 publications

Suggestive Evidence for Darwinian Selection against Asparagine-Linked Glycans of Plasmodium falciparum and Toxoplasma gondii

Suggestive Evidence for Darwinian Selection against Asparagine-Linked Glycans of Plasmodium falciparum and Toxoplasma gondii

Antimicrobial activity of lectins from Antimicrobial Activity of Lectins from Plants

Carbohydrate binding and resistance to proteolysis control insecticidal activity of Griffonia simplicifolia lectin II

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