A study on the distribution of Porphyromonas gingivalis repeated epitope in hemagglutinin/adhesion and hagA gingipains domain antigen and DNA in Alzheimer brains

Article

Author: Nara, Peter Lloyd

BACKGROUNDAlzheimer's disease (AD) is a progressive neuroinflammatory and neurodegenerative disease of the brain, defined by the accumulation and deposition of beta-amyloid, which has recently been identified as an antimicrobial peptide suggesting an infectious etiology. Specific bacterial infections and factors especially caused by the oral Keystone Pathogen-Porphyromonas gingivalis (Pg) in both humans and animal models have shown to initiate and chronically stimulate the systemic innate host defense systems and inflammasome. Overtime these compromise the integrity of the blood brain barrier, localize in the brain parenchyma neurons and supporting cells and through multiple inflammatory pathways and lead to activation of microglia and astrocytes.METHODA novel anti-pg bacterial monoclonal antibody currently in pre- and clinical development was used for all described work. Forty-six brain tissue samples (frontal and temporal biopsies) from 23 brain specimens (7 AD and 16 AMC) were subjected to PCR-based liquid hybridization assay to detect P. gingivalis DNA. All were negative for P. gingivalis DNA. Alzheimer brain sections from multiple functionally distinct anatomic regions and 15 different patient choroid plexus were tested by Porphyromonas gingivalis antigen-specific immuno-histochemistry.RESULTA unique Pg clinically relevant antigen was detected by IHC in multiple functionally distinct brain sections from all AD brains tested. This antigen was found with greatest intensity and frequency in the Fronto-temporal, Hippocampal lobes, Choroid plexus, Occipital and Cerebellar lobes. No P.g. DNA was found by PCR in 7 different AD brains with 46 different tissue samples from the frontal and temporal lobes. Three AD brains tested for both DNA and the novel Pg antigen and found negative for DNA but strongly positive by IHC. This Pg antigen was found in neurons, astrocytes, microglial and choroid ependyma lining cells in the brain. Pull down experiments demonstrated the same protein fragments. Some aged match controls wee also positive by IHC and not Pg DNA.CONCLUSIONThis is the first time for this clinically relevant, unique Pg antigen to be found in many AD brain tissues. Its role in systemic inflammatory diseases for Pg is well understood and now demonstrates that its most likely source is from OMVs of oral origin.

01 Nov 2014·Canadian Journal of MicrobiologyQ4 · BIOLOGY

Expression and characterization of single-chain variable fragment antibody against staphylococcal enterotoxin A in Escherichia coli

Q4 · BIOLOGY

Article

Author: Chen, Fusheng ; Chen, Weifeng ; Li, Jinquan ; Liu, Aiping ; Wang, Xiaohong ; Hu, Li

The staphylococcal enterotoxins (SEs) are potent gastrointestinal exotoxins synthesized by Staphylococcus aureus, which is responsible for various diseases including septicemia, food poisoning, and toxic shock syndrome, as well as bovine mastitis. Among them, staphylococcal enterotoxin A (SEA) is one of the most commonly present serotypes in staphylococcal food poisoning cases. In this study, the stable hybridoma 3C12 producing anti-SEA monoclonal antibody was established with an equilibrium dissociation constant (KD) of 1.48 × 10−8 mol·L−1, its ScFv-coding genes were obtained and then the anti-SEA single chain variable fragment (ScFv) protein was expressed in Escherichia coli. Characterization of the expressed target ScFv protein was analyzed by sodium dodecyl sulfate – polyacrylamide gel electrophoresis, Western blot, and enzyme-linked immunosorbent assay. The results demonstrated that the recombinant anti-SEA ScFv protein retained a specific binding activity for SEA, and the KD value of the soluble ScFv was about 3.75 × 10−7 mol·L−1. The overall yield of bioactive anti-SEA ScFv in E. coli flask culture was more than 10 mg·L−1.

01 Aug 2008·Cancer LettersQ1 · MEDICINE

Monoclonal antibody to cytokeratin VKIALEVEIATY sequence motif reduces plasminogen activation in breast tumour cells

Q1 · MEDICINE

Article

Author: Polona Jamnik ; Bojan Doljak ; Janko Kos ; Nataša Obermajer

Cytokeratins (CKs) are the main structural proteins of epithelial cells. Although they mainly form cytoplasmic structures, they are also localized at the plasma membrane or secreted from the cells. Some CKs are over-expressed in tumour cells and are used as diagnostic and prognostic biomarkers. A stable hybridoma cell line producing anti-cytokeratin monoclonal antibody (anti-CK MAb) was prepared after immunizing mice with breast cancer MCF-7 cell lysate. As shown by 2D electrophoresis, immunoblotting and mass spectroscopy, the monoclonal antibody recognizes an epitope on CK1, CK2, CK8, CK10 and CK18 in MCF-7 cells. To identify the binding site of the antibody three peptides of 12 amino acids were synthesized, each overlapping a 27 amino acid consensus sequence of the recognized CKs. Anti-CK MAb expressed high affinity for a dodecapeptide with the sequence VKIALEVEIATY, localized in the CK alpha-helical B2 domain, as shown by ELISA and surface plasmon resonance. Treatment of MCF-7 cells by anti-CK MAb impaired plasminogen activation and consequently invasiveness of the cells. Our results show that, besides their use in diagnosis, anti-cytokeratin antibodies could be used in therapy of invasive breast cancer.

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Indication	Highest Phase	Country/Location	Organization	Date
Infectious Diseases	Phase 1	US	Development Center for Biotechnology	30 Jan 2022

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