Isolation and characterization of conglutinin as an influenza A virus inhibitor

Wakamiya, Nobutaka; Okuno, Yoshinobu; Sasao, Fuyoko; Ueda, Shigeharu; Yoshimatsu, Kumiko; Naiki, Masaharu; Kurimura, Takashi

doi:10.1016/0006-291x(92)90440-v

Cited by 36 publications

(26 citation statements)

References 25 publications

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“…However, whether other animal serum collectins exert direct inhibitory effects against influenza A virus has not been definitely determined. We have previously determined the primary structure and the complement activating ability of bovine MBL and rabbit MBL [20,21], and characterized the biochemical and biological activities of BKg [29,30]. In this study, we investigated the direct antiviral activities of bovine MBL, rabbit MBL and BKg against influenza A virus.…”

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confidence: 99%

Anti-Influenza A Virus Activities of Mannan-Binding Lectins and Bovine Conglutinin

Kawai

Kase

Suzuki

et al. 2007

The Journal of Veterinary Medical Science

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ABSTRACT. Mannan-binding lectin (MBL) and bovine conglutinin (BKg) belong to the collectin family, which is involved in first-line host defense against various infectious agents. We have previously reported that human MBL inhibited type A influenza viral hemagglutination, infection and spreading to adjacent cells without complement activation. In this study, we investigated the direct antiviral activities of bovine MBL, rabbit MBL and BKg. All collectins used in this study inhibited viral infectivity and hemagglutination at concentrations of 0.02-0.3 µg/ml. They also demonstrated inhibitory activity against viral spreading. Like human MBL, bovine MBL and BKg showed antiviral activities at their physiological concentrations. These results suggest that mammalian MBLs and BKg may inhibit the spread of influenza A virus through the bloodstream. KEY WORDS: conglutinin, influenza A virus, mannan-binding lectin.

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confidence: 99%

Anti-Influenza A Virus Activities of Mannan-Binding Lectins and Bovine Conglutinin

Kawai

Kase

Suzuki

et al. 2007

The Journal of Veterinary Medical Science

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“…MBP can destroy bacteria through activation of the complement pathway (8) or by opsonization by collectin receptors (9). Conglutinin is a ␤-inhibitor of influenza A viruses that exhibits hemagglutination inhibition and neutralization activities (10,11). SP-A enhances the phagocytosis of bacteria by macrophages (12) and opsonizes herpes simplex virus (13).…”

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confidence: 99%

Molecular Cloning of a Novel Human Collectin from Liver (CL-L1)

Ohtani¹,

Suzuki²,

Eda³

et al. 1999

Journal of Biological Chemistry

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Collectins are a C-lectin family with collagen-like sequences and carbohydrate recognition domains. These proteins can bind to carbohydrate antigens of microorganisms and inhibit their infection by direct neutralization and agglutination, the activation of complement through the lectin pathway, and opsonization by collectin receptors. Here we report the cloning of a cDNA encoding human collectin from liver (CL-L1 (collectin liver 1)) that has typical collectin structural characteristics, consisting of an N-terminal cysteine-rich domain, a collagen-like domain, a neck domain, and a carbohydrate recognition domain. The cDNA has an insert of 831 base pairs coding for a protein of 277 amino acid residues. The deduced amino acid sequence shows that this collectin has a unique repeat of four lysine residues in its C-terminal area. Northern blot, Western blot, and reverse transcription-polymerase chain reaction analyses showed that CL-L1 is present mainly in liver as a cytosolic protein and at low levels in placenta. More sensitive analyses by reverse transcription-polymerase chain reactions showed that most tissues (except skeletal muscle) have CL-L1 mRNA. Zoo-blot analysis indicated that CL-L1 is limited to mammals and birds. A chromosomal localization study indicated that the CL-L1 gene localizes to chromosome 8q23-q24.1, different from chromosome 10 of other human collectin genes. Expression studies of fusion proteins lacking the collagen and N-terminal domains produced in Escherichia coli affirmed that CL-L1 binds mannose weakly. CL-L1 and recombinant CL-L1 fusion proteins do not bind to mannan columns. Analysis of the phylogenetic tree of CL-L1 and other collectins indicated that CL-L1 belongs to a fourth subfamily of collectins following the mannan-binding protein, surfactant protein A, and surfactant protein D subfamilies including bovine conglutinin and collectin-43 (CL-43). These findings indicate that CL-L1 may be involved in different biological functions.

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“…C-type lectins inhibit the haemagglutination activity of influenza A virus by binding to the high-mannose oligosaccharide near the sialic acid-binding site of viral HA [12]. This inhibition has been observed with MBP [30], conglutinin [13] and SP-D [17], which bind to the high-mannose oligosaccharide with its lectin domain. Although native SP-D exhibited HA inhibition activity, truncated SP-D was unable to inhibit haemagglutination, even when employed at higher concentrations (more than 20 µg\ml).…”

Section: Discussionmentioning

confidence: 98%

“…tivity towards influenza A viruses [12][13][14]. SP-A enhances the phagocytosis of bacteria [15] by alveolar macrophages and acts as an opsonin for herpes simplex virus [16].…”

Section: Introductionmentioning

confidence: 99%

Structure of a truncated human surfactant protein D is less effective in agglutinating bacteria than the native structure and fails to inhibit haemagglutination by influenza A virus

Eda

Suzuki

Kawai

et al. 1997

Biochemical Journal

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Surfactant protein D (SP-D) is a lung-specific protein that is synthesized and secreted by lung epithelial cells and is believed to play an important role in lung host defence. This protein belongs to the C-type lectin family, which is characterized by an Nterminal cysteine-rich domain, a collagen-like domain, a neck domain and a carbohydrate recognition domain (CRD). To elucidate the biological actions of this animal lectin against such pathogens as micro-organisms, the biological activities of a recombinant partial SP-D lacking a collagen-like domain were examined. A recombinant human SP-D, consisting of a short collagen region (two repeats of Gly-Xaa-Yaa amino acid sequences), the neck domain and the CRD, was expressed in Escherichia coli. The recombinant SP-D was purified on a nickel column and then on a maltose-agarose column. This protein can form a trimeric structure owing to the neck domain and exhibits sugar-binding activity and specificity similar to those of native human SP-D. The recombinant SP-D caused dose-dependent and calcium-dependent agglutination of E. coli Y1088. The agglutination titre (the concentration required to achieve a 50 %

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Isolation and characterization of conglutinin as an influenza A virus inhibitor

Cited by 36 publications

References 25 publications

Anti-Influenza A Virus Activities of Mannan-Binding Lectins and Bovine Conglutinin

Anti-Influenza A Virus Activities of Mannan-Binding Lectins and Bovine Conglutinin

Molecular Cloning of a Novel Human Collectin from Liver (CL-L1)

Structure of a truncated human surfactant protein D is less effective in agglutinating bacteria than the native structure and fails to inhibit haemagglutination by influenza A virus

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