A5069308432- Glycosylation and Glycoproteins Research
- Monoclonal and Polyclonal Antibodies Research
- Carbohydrate Chemistry and Synthesis
- Galectins and Cancer Biology
- Protein purification and stability
- Polysaccharides and Plant Cell Walls
- Viral Infectious Diseases and Gene Expression in Insects
- Polysaccharides Composition and Applications
- Toxin Mechanisms and Immunotoxins
- Ubiquitin and proteasome pathways
- Peptidase Inhibition and Analysis
- Advanced Proteomics Techniques and Applications
- Microbial Metabolites in Food Biotechnology
- Antimicrobial Peptides and Activities
- Autophagy in Disease and Therapy
- Biofuel production and bioconversion
- Cell Adhesion Molecules Research
- Invertebrate Immune Response Mechanisms
- Genomics and Phylogenetic Studies
- RNA and protein synthesis mechanisms
- Redox biology and oxidative stress
- Advanced Biosensing Techniques and Applications
- Histone Deacetylase Inhibitors Research
- Virus-based gene therapy research
- Erythrocyte Function and Pathophysiology
Center for Global Development
2018
Janssen (United States)
2013-2016
Janssen (Belgium)
2012-2014
Johnson & Johnson (United States)
2013
Biotechnology Research Center
2012
Albert Einstein College of Medicine
1995-2003
Sidney Kimmel Comprehensive Cancer Center
2003
Johns Hopkins University
2003
FibroGen (United States)
2002
Genentech
2000-2001
Immunoglobulins (IgG) are soluble serum glycoproteins in which the oligosaccharides play significant roles bioactivity and pharmacokinetics. Recombinant immuno-globulins (rIgG) produced different host cells by recombinant DNA technology becoming major therapeutic agents to treat life threatening diseases such as cancer. Since glycosylation is cell type specific, rIgGs contain patterns of could affect biological functions. In order determine extent this variation N-linked oligosaccharide...
Protein aggregation is of great concern to pharmaceutical formulations and has been implicated in several diseases. We engineered an anti-IL-13 monoclonal antibody CNTO607 for improved solubility. Three structure-based engineering approaches were employed this study: (i) modifying the isoelectric point (pI), (ii) decreasing overall surface hydrophobicity (iii) re-introducing N-linked carbohydrate moiety within a complementarity-determining region (CDR) sequence. A mutant was identified with...
There are currently ~25 recombinant full-length IgGs (rIgGs) in the market that have been approved by regulatory agencies as biotherapeutics to treat various human diseases. Most of these based on IgG1k framework and either chimeric, humanized or antibodies manufactured using Chinese hamster ovary (CHO) cells mouse myeloma expression system. Because CHO mammalian cells, rIgGs produced cell lines typically N-glycosylated at conserved asparagine (Asn) residues CH2 domain Fc, which is also case...
Therapeutic glycoproteins produced in different host cells by recombinant DNA technology often contain terminal GlcNAc and Gal residues. Such clear rapidly from the serum as a consequence of binding to mannose receptor and/or asialoglycoprotein liver. To increase half-life these glycoproteins, we carried out vitro glycosylation experiments using TNFR-IgG, an immunoadhesin molecule, model therapeutic glycoprotein. TNFR-IgG is disulfide-linked dimer polypeptide composed extracellular portion...
Covalently-linked glycans on proteins have many functional roles, some of which are still not completely understood. Antibodies a very specific glycan modification in the Fc region that is required for mediating immune effector functions. These typically highly heterogeneous structure, and this heterogeneity influenced by factors, such as type cellular host rate Ab secretion. Glycan can affect Fc-dependent activities antibodies. It has been shown recently increased sialylation result...
Since its discovery, the polymerase chain reaction (PCR) has fundamentally changed biological science. It made it possible to produce enormous amounts of DNA and detect specifically for first time. Large-scale scientific initiatives like Human Genome Project have been fuelled by PCR-based techniques. Nowadays, method is widely utilised researchers clinicians quickly sensitively perform complex genomic quantitative studies, clone sequence genes, diagnose disorders. Pathogen detection one most...
The complete structure for the core region of Campylobacter jejuni serotype O:2 lipopolysaccharide (LPS) was assigned through studies on derivatives liberated oligosaccharide (OS 2) and intact LPS. Structure determinations were performed using 1 H‐NMR spectroscopy, methylation supported by fast‐atom‐bombardment mass spectrometry linkage analysis gas chromatography/mass spectrometry, Smith degradation, oxidation with chromium trioxide. It concluded that chains had following structure: image
Low-Mr lipopolysaccharides (LPS) of Campylobacter jejuni reference strains for serotypes O:1, O:4, O:23, and O:36 were examined through the liberation core oligosaccharides by mild acid cleavage ketosidic linkage 3-deoxy-D-manno-2-octulosonic residues to lipid A moiety. The liberated chemical structure compositional analysis methylated in conjunction with fast atom bombardment-mass spectrometry permethylated oligosaccharide derivatives. results showed (i) that LPS contained short chains...
ABSTRACT Immunoglobulin G (IgG) antibodies are an integral part of the adaptive immune response that provide a direct link between humoral and cellular components system. Insights into relationships structure function human IgGs have prompted molecular engineering efforts to enhance or eliminate specific properties, such as Fc‐mediated effector functions. Human N‐glycosylation site at Asn297, located in second heavy chain constant region (CH2). The composition Fc glycan can substantial...
Glycosylation in the CH2 domain of Fc is required for immunoglobulins G (IgGs) to exhibit immune effector functions including complement-dependent cytotoxicity (CDC) and antibody-dependent (Ab-dependent) cellular (ADCC). We recently established that glycosylated Abs are more resistant papain digestion than non-glycosylated IgGs (Biochem. Biophys. Res. Commun. 2006, 341, 797-803). To test whether specific glycan structures affect Ab resistance papain, we used vitro glycoengineering methods...
The successful development of antibody therapeutics depends on the molecules having properties that are suitable for manufacturing, as well use by patients. Because high solubility is a desirable property antibodies, screening has become an essential step during early candidate selection process. In considering process, we formed hypothesis hybridoma antibodies filtered nature to possess and tested this using large number murine hybridoma-derived antibodies. Using cross-interaction...
N-Acetylglucosaminyltransferase III (GlcNAc-TIII), the product of Mgat3 gene, transfers bisecting GlcNAc to core mannose complexN-glycans. The addition this residue is regulated during development and has functional consequences for receptor signaling, cell adhesion, tumor progression. Mice homozygous a null mutation at locus (Mgat3 Δ) or targeted in theMgat3 gene (previously called neo , but herein renamed T37 because allele generates inactive GlcNAc-TIII ∼37 kDa) were found exhibit...
The lectin from the seeds of Dioclea grandiflora (DGL) is a Man/Glc‐specific tetrameric protein with physical and saccharide‐binding properties reported to be similar that jack bean concanavalin A (ConA). Unlike other plant lectins, both DGL ConA bind high affinity core trimannoside moiety, 3,6‐di‐ O ‐(α‐ d ‐mannopyranosyl)‐α‐ ‐mannopyranoside, which present in all asparagine‐linked carbohydrates. In study, hemagglutination inhibition techniques have been used investigate binding series...