Erratum to: High-Mannose Specific Lectin and Its Recombinants from a Carrageenophyta Kappaphycus alvarezii Represent a Potent Anti-HIV Activity Through High-Affinity Binding to the Viral Envelope Glycoprotein gp120
Autor: | Koji Imamura, Kanji Hori, Hiromi Shibata, Takemasa Sakaguchi, Makoto Hirayama |
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Jazyk: | angličtina |
Rok vydání: | 2016 |
Předmět: |
Specific lectin
Anti-HIV Agents Gene Expression Oligosaccharides HIV Envelope Protein gp120 01 natural sciences Applied Microbiology and Biotechnology Jurkat Cells Kappaphycus alvarezii Lectins Escherichia coli Humans Protein Isoforms Amino Acid Sequence Cloning Molecular biology 010405 organic chemistry Algal Proteins Virus Internalization biology.organism_classification Recombinant Proteins 0104 chemical sciences 010404 medicinal & biomolecular chemistry Biochemistry Carbohydrate Sequence Rhodophyta HIV-1 High mannose Erratum Mannose Sequence Alignment Protein Binding |
Zdroj: | Marine Biotechnology (New York, N.y.) |
ISSN: | 1436-2236 1436-2228 |
Popis: | We previously reported that a high-mannose binding lectin KAA-2 from the red alga Kappaphycus alvarezii, which is an economically important species and widely cultivated as a source of carrageenans, had a potent anti-influenza virus activity. In this study, the full-length sequences of two KAA isoforms, KAA-1 and KAA-2, were elucidated by a combination of peptide mapping and cDNA cloning. They consisted of four internal tandem-repeated domains, which are conserved in high-mannose specific lectins from lower organisms, including a cyanobacterium Oscillatoria agardhii and a red alga Eucheuma serra. Using an Escherichia coli expression system, an active recombinant form of KAA-1 (His-tagged rKAA-1) was successfully generated in the yield of 115 mg per a litter of culture. In a detailed oligosaccharide binding analysis by a centrifugal ultrafiltration-HPLC method with 27 pyridylaminated oligosaccharides, His-tagged rKAA-1 and rKAA-1 specifically bound to high-mannose N-glycans with an exposed α1-3 mannose in the D2 arm as the native lectin did. Predicted from oligosaccharide-binding specificity, a surface plasmon resonance analysis revealed that the recombinants exhibit strong interaction with gp120, a heavily glycosylated envelope glycoprotein of HIV with high association constants (1.48-1.61 × 10(9) M(-1)). Native KAAs and the recombinants inhibited the HIV-1 entry at IC50s of low nanomolar levels (7.3-12.9 nM). Thus, the recombinant proteins would be useful as antiviral reagents targeting the viral surface glycoproteins with high-mannose N-glycans, and the cultivated alga K. alvarezii could also be a good source of not only carrageenans but also this functional lectin(s). |
Databáze: | OpenAIRE |
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