Crystal Structure of Abrin-a at 2.14 Å

Tahirov, T.H.; Lu, Tian‐Huey; Liaw, Yen-Chywan; Chen, Yung Liang; Lin, Jung‐Yaw

doi:10.1006/jmbi.1995.0382

Cited by 145 publications

(62 citation statements)

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“…We postulate that the glycan on Gn is somehow shielded or hidden by the Gc protein in the Gn-Gc heterodimer and may not be easily accessed by Golgi enzymes for terminal modification. The first N-glycan on abrin-a, a type II ribosomeinactivating protein from the seeds of Abrus precatorius, works as a bridge between abrin-a molecules, connecting them as a linear polymer (49); perhaps the glycan on N60 acts in the same way to promote formation of the Gn-Gc heterodimer.…”

Section: Discussionmentioning

confidence: 99%

Role of N-Linked Glycans on Bunyamwera Virus Glycoproteins in Intracellular Trafficking, Protein Folding, and Virus Infectivity

Shi

Brauburger

Elliott

2005

J Virol

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The membrane glycoproteins (Gn and Gc) of Bunyamwera virus (BUN, family Bunyaviridae) contain three potential sites for the attachment of N-linked glycans: one site (N60) on Gn and two (N624 and N1169) on Gc. We determined that all three sites are glycosylated. Digestion of the glycoproteins with endo-␤-N-acetylglucosaminidase H (endo H) or peptide:N-glycosidase F revealed that Gn and Gc differ significantly in their glycan status and that late in infection Gc glycans remain endo H sensitive. The roles of the N-glycans in intracellular trafficking of the glycoproteins to the Golgi, protein folding, and virus replication were investigated by mutational analysis and confocal immunofluorescence. Elimination of the glycan on Gn, by changing N60 to a Q residue, resulted in the protein misfolding and failure of both Gn and Gc proteins to traffic to the Golgi complex. We were unable to rescue a viable virus by reverse genetics from a cDNA containing the N60Q mutation. In contrast, mutant Gc proteins lacking glycans on either N624 or N1169, or both sites, were able to target to the Golgi. Gc proteins containing mutations N624Q and N1169Q acquired endo H resistance. Three viable N glycosylation-site-deficient viruses, lacking glycans on one site or both sites on Gc, were created by reverse genetics. The viability of these recombinant viruses and analysis of growth kinetics indicates that the glycans on Gc are not essential for BUN replication, but they do contribute to the efficiency of virus infection.

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Section: Discussionmentioning

confidence: 99%

Role of N-Linked Glycans on Bunyamwera Virus Glycoproteins in Intracellular Trafficking, Protein Folding, and Virus Infectivity

Shi

Brauburger

Elliott

2005

J Virol

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“…Several mushroom ricin B-like lectins have been identified (5), and crystal structures have been solved for Laetiporus sulfureus lectin (LSL) 2 (11), a lectin from mushroom Marasmius oreades (MOA) (12) and for Polyporus squamosus lectin (PSL) (13). Similarly to toxic proteins like ricin (14), abrin (15), and related plant toxins (16), these mushroom proteins are chimerolectins, containing a nonlectin domain at the C terminus in addition to the lectin domain at the N terminus. LSL contains a pore-forming module (11), whereas a cysteine protease domain, which also serves as a dimerization interface, is present in MOA and PSL (12,13,17).…”

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confidence: 99%

Bivalent Carbohydrate Binding Is Required for Biological Activity of Clitocybe nebularis Lectin (CNL), the N,N′-Diacetyllactosediamine (GalNAcβ1–4GlcNAc, LacdiNAc)-specific Lectin from Basidiomycete C. nebularis

Pohleven

Renko

Magister

et al. 2012

Journal of Biological Chemistry

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Background: Lectins are carbohydrate-binding proteins that exert their activity by binding to specific glycoreceptors. Results: Clitocybe nebularis lectin (CNL) showed biological activity, although its nonsugar-binding and monovalent mutants were inactive. Conclusion:The bivalent carbohydrate-binding property of CNL is essential for its activity. Significance: Understanding the interactions of lectins with glycans and elucidating their modes of action are necessary for their application in biomedicine.

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“…The three-dimensional structures of various type 2 RIPs are available (e.g. abrin [26], ricin [27], mistletoe lectin [28], ebulin [29], and Himalayan RIP [30]). The three-dimensional model of volkensin was obtained by using the ricin structure as template, whose sequence showed the highest percentage of identity (48%).…”

Section: Resultsmentioning

confidence: 99%

Structural analysis of toxic volkensin, a type 2 ribosome inactivating protein from Adenia volkensii Harm (kilyambiti plant): Molecular modeling and surface analysis by computational methods and limited proteolysis

Severino¹,

Paiardini

Pascarella

et al. 2009

International Journal of Biological Macromolecules

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Crystal Structure of Abrin-a at 2.14 Å

Cited by 145 publications

References 0 publications

Role of N-Linked Glycans on Bunyamwera Virus Glycoproteins in Intracellular Trafficking, Protein Folding, and Virus Infectivity

Role of N-Linked Glycans on Bunyamwera Virus Glycoproteins in Intracellular Trafficking, Protein Folding, and Virus Infectivity

Bivalent Carbohydrate Binding Is Required for Biological Activity of Clitocybe nebularis Lectin (CNL), the N,N′-Diacetyllactosediamine (GalNAcβ1–4GlcNAc, LacdiNAc)-specific Lectin from Basidiomycete C. nebularis

Structural analysis of toxic volkensin, a type 2 ribosome inactivating protein from Adenia volkensii Harm (kilyambiti plant): Molecular modeling and surface analysis by computational methods and limited proteolysis

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