A5043176126- HIV Research and Treatment
- Glycosylation and Glycoproteins Research
- Carbohydrate Chemistry and Synthesis
- HIV/AIDS drug development and treatment
- Cytomegalovirus and herpesvirus research
- Probiotics and Fermented Foods
- Redox biology and oxidative stress
- Tryptophan and brain disorders
- Vitamin C and Antioxidants Research
- Reproductive tract infections research
- Hepatitis B Virus Studies
- Aquaculture disease management and microbiota
- Mosquito-borne diseases and control
- HIV/AIDS Research and Interventions
- Endoplasmic Reticulum Stress and Disease
- Adenosine and Purinergic Signaling
- Hepatitis C virus research
Rega Institute for Medical Research
2013-2019
KU Leuven
2013-2019
Brazil has one of the largest biodiversities in world. The search for new natural products extracted from Brazilian flora may lead to discovery novel drugs with potential treat infectious and other diseases. Here, we have investigated 9 lectins purified Northeastern flora, both leguminous species: Canavalia brasiliensis (ConBr), C. maritima (ConM), Dioclea lasiocarpa (DLasiL) D. sclerocarpa (DSclerL), algae Amansia multifida (AML), Bryothamniom seaforthii (BSL), Hypnea musciformis (HML),...
N-linked glycans covering the surface of HIV-1 glycoprotein gp120 are major importance for correct folding this glycoprotein. Of the, on average, 24 present gp120, glycan at Asn260 was reported to be essential expression and gp41 in virus particle deletion N260 heavily compromised infectivity. We show here that gp160 containing N260Q mutation reaches Golgi apparatus during biosynthesis. Using pulse-chase experiments with [35S] methionine/cysteine, we oxidative slightly delayed case mutant...
The HIV envelope glycoprotein gp120 contains nine disulphide bridges and is highly glycosylated, carrying on average 24 N-linked glycans. Using a probability calculation, we here demonstrate that there co-localization of glycans in HIV-1 gp120, with predominance close proximity to bridges, at the C-terminal side involved cysteines. Also, N-glycans are frequently found immediately adjacent N-terminal In contrast, positions to, but not neighboring seem be disfavored Such pronounced was also...
Background The entry of HIV into its host cell is an interesting target for chemotherapeutic intervention in the life-cycle virus. During entry, reduction disulfide bridges viral envelope glycoprotein gp120 by cellular oxidoreductases crucial. thioredoxin reductase-1 plays important role this oxidoreduction process recycling electrons to thioredoxin-1. Therefore, inhibitors may inhibit during HIV-1 entry. In present study, tellurium-based were investigated as potential Results...
A selection of carbohydrate-binding agents (CBAs) with different glycan specificities were evaluated for their inhibitory effect against HIV infection and transmission, interaction vaginal commensal bacteria. Several assays used the antiviral evaluation: (i) cell-free virus human CD4+ T lymphocyte C8166 cells; (ii) syncytium formation in co-cultures persistently HIV-1-infected HUT-78/HIV-1 non-infected SupT1 (iii) DC-SIGN-directed capture HIV-1 particles; (iv) transmission DC-SIGN-captured...
Carbohydrate-binding agents (CBAs) are potent antiretroviral compounds that target the N-glycans on HIV-1 envelope glycoproteins. The development of phenotypic resistance to CBAs by virus is accompanied deletion multiple N-linked glycans surface glycoprotein gp120. Recently, also an N-glycan transmembrane gp41 was shown be deleted during CBA development. We generated mutants lacking and determined influence these glycan deletions viral phenotype (infectivity, CD4 binding, incorporation in...
We investigated the effect of combining two potent carbohydrate-binding agents (CBAs) with a complementary resistance profile (based on different N-glycan deletion selections in HIV envelope glycoprotein gp120) drug development and viral fitness. A long-term selection procedure was used to obtain virus strains resistant mannose-specific Hippeastrum hybrid agglutinin (HHA), mannose-recognizing monoclonal antibody 2G12 combination both compounds. The env genes mutant viruses were sequenced...
Carbohydrate-binding agents (CBAs) are potent antiretroviral compounds that target the N-glycans on HIV-1 envelope glycoproteins. The development of phenotypic resistance to CBAs by virus is accompanied deletion multiple N-linked glycans surface glycoprotein gp120. Recently, also an N-glycan transmembrane gp41 was shown be deleted during CBA development. We generated mutants lacking and determined influence these glycan deletions viral phenotype (infectivity, CD4 binding, incorporation in...