Monovalent Lectin Microvirin Utilizes Hydropathic Recognition of HIV-1 Env for Inhibition of Virus Cell Infection
Microvirin is a lectin molecule known to have monovalent interaction with glycoprotein gp120. A previously reported high-resolution structural analysis defines the mannobiose-binding cavity of Microvirin. Nonetheless, structure does not directly define the energetics of binding contributions of prot...
Saved in:
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-01-01
|
| Series: | Viruses |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1999-4915/17/1/82 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832587308388319232 |
|---|---|
| author | Bibek Parajuli Kriti Acharya Harry Charles Bach Shiyu Zhang Cameron F. Abrams Irwin Chaiken |
| author_facet | Bibek Parajuli Kriti Acharya Harry Charles Bach Shiyu Zhang Cameron F. Abrams Irwin Chaiken |
| author_sort | Bibek Parajuli |
| collection | DOAJ |
| description | Microvirin is a lectin molecule known to have monovalent interaction with glycoprotein gp120. A previously reported high-resolution structural analysis defines the mannobiose-binding cavity of Microvirin. Nonetheless, structure does not directly define the energetics of binding contributions of protein contact residues. To better understand the nature of the MVN-Env glycan interaction, we used mutagenesis to evaluate the residue contributions to the mannobiose binding site of MVN that are important for Env gp120 glycan binding. MVN binding site amino acid residues were individually replaced by alanine, and the resulting purified recombinant MVN variants were examined for gp120 interaction using competition Enzyme-Linked Immunosorbent Assay (ELISA), biosensor surface plasmon resonance, calorimetry, and virus neutralization assays. Our findings highlight the role of both uncharged polar and non-polar residues in forming a hydropathic recognition site for the monovalent glycan engagement of Microvirin, in marked contrast to the charged residues utilized in the two Cyanovirin-N (CVN) glycan-binding sites. |
| format | Article |
| id | doaj-art-ad84e3485c294d408f38a09018e02e7d |
| institution | Kabale University |
| issn | 1999-4915 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj-art-ad84e3485c294d408f38a09018e02e7d2025-01-24T13:52:31ZengMDPI AGViruses1999-49152025-01-011718210.3390/v17010082Monovalent Lectin Microvirin Utilizes Hydropathic Recognition of HIV-1 Env for Inhibition of Virus Cell InfectionBibek Parajuli0Kriti Acharya1Harry Charles Bach2Shiyu Zhang3Cameron F. Abrams4Irwin Chaiken5Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USADepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USADepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USADepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USADepartment of Chemical and Biological Engineering, Drexel University, Philadelphia, PA 19104, USADepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USAMicrovirin is a lectin molecule known to have monovalent interaction with glycoprotein gp120. A previously reported high-resolution structural analysis defines the mannobiose-binding cavity of Microvirin. Nonetheless, structure does not directly define the energetics of binding contributions of protein contact residues. To better understand the nature of the MVN-Env glycan interaction, we used mutagenesis to evaluate the residue contributions to the mannobiose binding site of MVN that are important for Env gp120 glycan binding. MVN binding site amino acid residues were individually replaced by alanine, and the resulting purified recombinant MVN variants were examined for gp120 interaction using competition Enzyme-Linked Immunosorbent Assay (ELISA), biosensor surface plasmon resonance, calorimetry, and virus neutralization assays. Our findings highlight the role of both uncharged polar and non-polar residues in forming a hydropathic recognition site for the monovalent glycan engagement of Microvirin, in marked contrast to the charged residues utilized in the two Cyanovirin-N (CVN) glycan-binding sites.https://www.mdpi.com/1999-4915/17/1/82SPRepitopeBiacorecalorimetrySensorgramELISA |
| spellingShingle | Bibek Parajuli Kriti Acharya Harry Charles Bach Shiyu Zhang Cameron F. Abrams Irwin Chaiken Monovalent Lectin Microvirin Utilizes Hydropathic Recognition of HIV-1 Env for Inhibition of Virus Cell Infection Viruses SPR epitope Biacore calorimetry Sensorgram ELISA |
| title | Monovalent Lectin Microvirin Utilizes Hydropathic Recognition of HIV-1 Env for Inhibition of Virus Cell Infection |
| title_full | Monovalent Lectin Microvirin Utilizes Hydropathic Recognition of HIV-1 Env for Inhibition of Virus Cell Infection |
| title_fullStr | Monovalent Lectin Microvirin Utilizes Hydropathic Recognition of HIV-1 Env for Inhibition of Virus Cell Infection |
| title_full_unstemmed | Monovalent Lectin Microvirin Utilizes Hydropathic Recognition of HIV-1 Env for Inhibition of Virus Cell Infection |
| title_short | Monovalent Lectin Microvirin Utilizes Hydropathic Recognition of HIV-1 Env for Inhibition of Virus Cell Infection |
| title_sort | monovalent lectin microvirin utilizes hydropathic recognition of hiv 1 env for inhibition of virus cell infection |
| topic | SPR epitope Biacore calorimetry Sensorgram ELISA |
| url | https://www.mdpi.com/1999-4915/17/1/82 |
| work_keys_str_mv | AT bibekparajuli monovalentlectinmicrovirinutilizeshydropathicrecognitionofhiv1envforinhibitionofviruscellinfection AT kritiacharya monovalentlectinmicrovirinutilizeshydropathicrecognitionofhiv1envforinhibitionofviruscellinfection AT harrycharlesbach monovalentlectinmicrovirinutilizeshydropathicrecognitionofhiv1envforinhibitionofviruscellinfection AT shiyuzhang monovalentlectinmicrovirinutilizeshydropathicrecognitionofhiv1envforinhibitionofviruscellinfection AT cameronfabrams monovalentlectinmicrovirinutilizeshydropathicrecognitionofhiv1envforinhibitionofviruscellinfection AT irwinchaiken monovalentlectinmicrovirinutilizeshydropathicrecognitionofhiv1envforinhibitionofviruscellinfection |