About: 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

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About: 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 Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	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
Creator	Hirayama, Makoto Hori, Kanji Sakaguchi, Takemasa Imamura, Koji Shibata, Hiromi
Source	PMC
abstract	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 complementary DNA (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 liter 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 IC(50)s 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).
has issue date	2015-11-23(xsd:dateTime)
bibo:doi	10.1007/s10126-015-9677-1
bibo:pmid	26593063
has license	no-cc
sha1sum (hex)	b7575ec6aa09493a4b856bdeccdccf263c3312ca
schema:url	https://doi.org/10.1007/s10126-015-9677-1
resource representing a document's title	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
has PubMed Central identifier	PMC7088233
has PubMed identifier	26593063
schema:publication	Mar Biotechnol (NY)
resource representing a document's body	covid:b7575ec6aa09493a4b856bdeccdccf263c3312ca#body_text
is schema:about of	named entity 'α1-' named entity 'red alga' named entity 'targeting' named entity 'Oscillatoria' named entity 'high' named entity 'anti-influenza' named entity 'culture' named entity 'surface plasmon' named entity 'Envelope Glycoprotein gp120' named entity 'VIRAL ENVELOPE' named entity 'INCLUDING' named entity 'EUCHEUMA SERRA' named entity 'LENGTH' named entity 'HIV-1' named entity 'GENERATED' named entity 'EXPRESSION SYSTEM' named entity 'STUDY' named entity 'STRONG INTERACTION' named entity 'LOWER ORGANISMS' named entity 'DETAILED' named entity 'INHIBITED' named entity 'COMPLEMENTARY DNA' named entity 'TAGGED' named entity 'USING' named entity 'SPECIES' named entity 'BUT' named entity '9710' named entity 'NANOMOLAR' named entity 'PREVIOUSLY' named entity 'OLIGOSACCHARIDES' named entity 'ACTIVITY' named entity 'MANNOSE BINDING LECTIN' named entity '921' named entity 'B11' named entity 'HIGH' named entity 'ALGA' named entity 'BINDING SPECIFICITY' named entity 'ANTIVIRAL' named entity '28S' named entity 'KAA' named entity 'ISOFORMS' named entity 'ASSOCIATION' named entity '115' named entity 'METHOD' named entity '287' named entity 'KAPPAPHYCUS ALVAREZII' named entity 'SURFACE' named entity 'LECTIN' named entity 'BINDING ANALYSIS' named entity 'COMBINATION' named entity 'RECOMBINANTS' named entity 'CENTRIFUGAL' named entity 'GOOD' named entity 'SPECIFIC' named entity 'CONSTANTS' named entity 'REPORTED' named entity 'LECTINS' named entity 'GLYCOSYLATED' named entity 'RECOMBINANT' named entity 'HIS-' named entity 'ACTIVE' named entity 'OSCILLATORIA AGARDHII' named entity 'ESCHERICHIA COLI' named entity 'SEQUENCES' named entity 'CYANOBACTERIUM' named entity 'USEFUL' named entity 'VIRAL' named entity 'ECONOMICALLY IMPORTANT' named entity 'ENTRY' named entity 'REAGENTS' named entity 'ENVELOPE GLYCOPROTEIN' named entity 'MANNOSE SPECIFIC LECTIN' named entity 'ENVELOPE GLYCOPROTEIN' named entity 'YIELD' named entity 'KAPPAPHYCUS ALVAREZII' named entity 'AFFINITY' named entity 'GP120'

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