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Legume Lectins Inhibit Human Parainfluenza Virus Type 2 Infection by Interfering with the Entr
Three lectins with different sugar binding specificities were investigated for anti-viral activity against human parainfluenza virus type 2 (hPIV-2). The lectins, concanavalin A (Con A), lens culinaris agglutinin (LCA) and peanut agglutinin (PNA), inhibited cell fusion and hemadsorption induced by h...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3407897/ https://www.ncbi.nlm.nih.gov/pubmed/22852043 http://dx.doi.org/10.3390/v4071104 |
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author | Uematsu, Jun Koyama, Aoi Takano, Sayaka Ura, Yukari Tanemura, Miho Kihira, Sahoko Yamamoto, Hidetaka Kawano, Mitsuo Tsurudome, Masato O’Brien, Myles Komada, Hiroshi |
author_facet | Uematsu, Jun Koyama, Aoi Takano, Sayaka Ura, Yukari Tanemura, Miho Kihira, Sahoko Yamamoto, Hidetaka Kawano, Mitsuo Tsurudome, Masato O’Brien, Myles Komada, Hiroshi |
author_sort | Uematsu, Jun |
collection | PubMed |
description | Three lectins with different sugar binding specificities were investigated for anti-viral activity against human parainfluenza virus type 2 (hPIV-2). The lectins, concanavalin A (Con A), lens culinaris agglutinin (LCA) and peanut agglutinin (PNA), inhibited cell fusion and hemadsorption induced by hPIV-2. Virus nucleoprotein (NP) gene synthesis was largely inhibited, but fusion (F) and hemagglutinin-neuraminidase (HN) gene syntheses were not. An indirect immunofluorescence study showed that Con A inhibited virus NP, F and HN protein syntheses, but LCA did not completely inhibit them, and that PNA inhibited only NP protein synthesis. Using a recombinant green fluorescence protein-expressing hPIV-2, without matrix protein (rghPIV-2ΔM), it was found that virus entry into the cells was not completely prevented. The lectins considerably reduced the number of viruses released compared with that of virus infected cells. The lectins bound to cell surface within 10 min, and many aggregates were observed at 30 min. Con A and LCA slightly disrupted actin microfilaments and microtubules, but PNA had almost no effect on them. These results indicated that the inhibitory effects of the lectins were caused mainly by the considerable prevention of virus adsorption to the cells by the lectin binding to their receptors. |
format | Online Article Text |
id | pubmed-3407897 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-34078972012-07-31 Legume Lectins Inhibit Human Parainfluenza Virus Type 2 Infection by Interfering with the Entr Uematsu, Jun Koyama, Aoi Takano, Sayaka Ura, Yukari Tanemura, Miho Kihira, Sahoko Yamamoto, Hidetaka Kawano, Mitsuo Tsurudome, Masato O’Brien, Myles Komada, Hiroshi Viruses Article Three lectins with different sugar binding specificities were investigated for anti-viral activity against human parainfluenza virus type 2 (hPIV-2). The lectins, concanavalin A (Con A), lens culinaris agglutinin (LCA) and peanut agglutinin (PNA), inhibited cell fusion and hemadsorption induced by hPIV-2. Virus nucleoprotein (NP) gene synthesis was largely inhibited, but fusion (F) and hemagglutinin-neuraminidase (HN) gene syntheses were not. An indirect immunofluorescence study showed that Con A inhibited virus NP, F and HN protein syntheses, but LCA did not completely inhibit them, and that PNA inhibited only NP protein synthesis. Using a recombinant green fluorescence protein-expressing hPIV-2, without matrix protein (rghPIV-2ΔM), it was found that virus entry into the cells was not completely prevented. The lectins considerably reduced the number of viruses released compared with that of virus infected cells. The lectins bound to cell surface within 10 min, and many aggregates were observed at 30 min. Con A and LCA slightly disrupted actin microfilaments and microtubules, but PNA had almost no effect on them. These results indicated that the inhibitory effects of the lectins were caused mainly by the considerable prevention of virus adsorption to the cells by the lectin binding to their receptors. MDPI 2012-06-29 /pmc/articles/PMC3407897/ /pubmed/22852043 http://dx.doi.org/10.3390/v4071104 Text en © 2012 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Uematsu, Jun Koyama, Aoi Takano, Sayaka Ura, Yukari Tanemura, Miho Kihira, Sahoko Yamamoto, Hidetaka Kawano, Mitsuo Tsurudome, Masato O’Brien, Myles Komada, Hiroshi Legume Lectins Inhibit Human Parainfluenza Virus Type 2 Infection by Interfering with the Entr |
title | Legume Lectins Inhibit Human Parainfluenza Virus Type 2 Infection by Interfering with the Entr |
title_full | Legume Lectins Inhibit Human Parainfluenza Virus Type 2 Infection by Interfering with the Entr |
title_fullStr | Legume Lectins Inhibit Human Parainfluenza Virus Type 2 Infection by Interfering with the Entr |
title_full_unstemmed | Legume Lectins Inhibit Human Parainfluenza Virus Type 2 Infection by Interfering with the Entr |
title_short | Legume Lectins Inhibit Human Parainfluenza Virus Type 2 Infection by Interfering with the Entr |
title_sort | legume lectins inhibit human parainfluenza virus type 2 infection by interfering with the entr |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3407897/ https://www.ncbi.nlm.nih.gov/pubmed/22852043 http://dx.doi.org/10.3390/v4071104 |
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