A recombinant human immunoglobulin with coherent avidity to hepatitis B virus surface antigens of various viral genotypes and clinical mutants.
The hepatitis B virus (HBV) envelope is composed of a lipid bilayer and three glycoproteins, referred to as the large (L), middle (M), and small (S) hepatitis B virus surface antigens (HBsAg). S protein constitutes the major portion of the viral envelope and an even greater proportion of subviral pa...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2020-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0236704 |
| _version_ | 1818678422164996096 |
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| author | Gi Uk Jeong Byung-Yoon Ahn Jaesung Jung Hyunjin Kim Tae-Hee Kim Woohyun Kim Ara Lee Kyuhyun Lee Jung-Hwan Kim |
| author_facet | Gi Uk Jeong Byung-Yoon Ahn Jaesung Jung Hyunjin Kim Tae-Hee Kim Woohyun Kim Ara Lee Kyuhyun Lee Jung-Hwan Kim |
| author_sort | Gi Uk Jeong |
| collection | DOAJ |
| description | The hepatitis B virus (HBV) envelope is composed of a lipid bilayer and three glycoproteins, referred to as the large (L), middle (M), and small (S) hepatitis B virus surface antigens (HBsAg). S protein constitutes the major portion of the viral envelope and an even greater proportion of subviral particles (SVP) that circulate in the blood. Recombinant S proteins are currently used as a preventive vaccine, while plasma fractions isolated from vaccinated people, referred to as hepatitis B immune globulin (HBIG), are used for short-term prophylaxis. Here, we characterized a recombinant human IgG1 type anti-S antibody named Lenvervimab regarding its binding property to a variety of cloned S antigens. Immunochemical data showed an overall consistent avidity of the antibody to S antigens of most viral genotypes distributed worldwide. Further, antibody binding was not affected by the mutations in the antigenic 'a' determinant found in many clinical variants, including the immune escape mutant G145R. In addition, mutations in the S gene sequence that confer drug resistance to the viral polymerase did not interfere with the antibody binding. These results support for a preventive use of the antibody against HBV infection. |
| first_indexed | 2024-12-17T09:15:00Z |
| format | Article |
| id | doaj.art-14360367fc4549cca288735e71be9217 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-17T09:15:00Z |
| publishDate | 2020-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-14360367fc4549cca288735e71be92172022-12-21T21:55:01ZengPublic Library of Science (PLoS)PLoS ONE1932-62032020-01-01158e023670410.1371/journal.pone.0236704A recombinant human immunoglobulin with coherent avidity to hepatitis B virus surface antigens of various viral genotypes and clinical mutants.Gi Uk JeongByung-Yoon AhnJaesung JungHyunjin KimTae-Hee KimWoohyun KimAra LeeKyuhyun LeeJung-Hwan KimThe hepatitis B virus (HBV) envelope is composed of a lipid bilayer and three glycoproteins, referred to as the large (L), middle (M), and small (S) hepatitis B virus surface antigens (HBsAg). S protein constitutes the major portion of the viral envelope and an even greater proportion of subviral particles (SVP) that circulate in the blood. Recombinant S proteins are currently used as a preventive vaccine, while plasma fractions isolated from vaccinated people, referred to as hepatitis B immune globulin (HBIG), are used for short-term prophylaxis. Here, we characterized a recombinant human IgG1 type anti-S antibody named Lenvervimab regarding its binding property to a variety of cloned S antigens. Immunochemical data showed an overall consistent avidity of the antibody to S antigens of most viral genotypes distributed worldwide. Further, antibody binding was not affected by the mutations in the antigenic 'a' determinant found in many clinical variants, including the immune escape mutant G145R. In addition, mutations in the S gene sequence that confer drug resistance to the viral polymerase did not interfere with the antibody binding. These results support for a preventive use of the antibody against HBV infection.https://doi.org/10.1371/journal.pone.0236704 |
| spellingShingle | Gi Uk Jeong Byung-Yoon Ahn Jaesung Jung Hyunjin Kim Tae-Hee Kim Woohyun Kim Ara Lee Kyuhyun Lee Jung-Hwan Kim A recombinant human immunoglobulin with coherent avidity to hepatitis B virus surface antigens of various viral genotypes and clinical mutants. PLoS ONE |
| title | A recombinant human immunoglobulin with coherent avidity to hepatitis B virus surface antigens of various viral genotypes and clinical mutants. |
| title_full | A recombinant human immunoglobulin with coherent avidity to hepatitis B virus surface antigens of various viral genotypes and clinical mutants. |
| title_fullStr | A recombinant human immunoglobulin with coherent avidity to hepatitis B virus surface antigens of various viral genotypes and clinical mutants. |
| title_full_unstemmed | A recombinant human immunoglobulin with coherent avidity to hepatitis B virus surface antigens of various viral genotypes and clinical mutants. |
| title_short | A recombinant human immunoglobulin with coherent avidity to hepatitis B virus surface antigens of various viral genotypes and clinical mutants. |
| title_sort | recombinant human immunoglobulin with coherent avidity to hepatitis b virus surface antigens of various viral genotypes and clinical mutants |
| url | https://doi.org/10.1371/journal.pone.0236704 |
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