Unlock instant, AI-driven research and patent intelligence for your innovation.

Inhibition of viral infection using monovalent antigen-binding proteins

A technology that binds proteins and virus infection, and is applied in antiviral agents, antiviral immunoglobulins, antibodies, etc., and can solve the problems of not being economically attractive, not being obtained, not being able to provide, etc.

Inactive Publication Date: 2002-05-29
UNILEVER NV
View PDF4 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, this approach failed to provide a commercially viable solution to the problem
Not only was it not economically attractive to produce antibodies in this way, but the addition of colostrum to milk was not approved by the relevant regulatory authorities

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Inhibition of viral infection using monovalent antigen-binding proteins
  • Inhibition of viral infection using monovalent antigen-binding proteins
  • Inhibition of viral infection using monovalent antigen-binding proteins

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0062] Example 1 Induction of Humoral Immune Response in Llama

[0063]The phage P2 of Lactococcus lactis (1:9V / V, antigen in water: Specol (Bokhout et al. (1981), Immunology (Immunol.) Immunopathology (Immunopathology) .), 2, 491-500; Bokhout et al. (1986), Infectious Diseases (Infect.Dis.), 161-168).Each immunization site injects 0.75-1.5ml of water-in-oil emulsion containing 200μg phage protein (about 6*10 13 pfu). Immunizations were given on the following schedule: a second immunization three weeks after the first injection, and a third immunization two weeks after the second injection. The immune response was then detected by ELISA on maxi-sorbplates (coating solution 10 10 pfu / ml was titrated on serum samples of phages diluted with phosphate buffered saline). After incubation with the sera, polyclonal rabbit-anti-llama antisera (obtained by immunizing rabbits with llama immunoglobulins purified on ProtA and ProtG columns; ID-DLO) combined with horseradish peroxidized...

Embodiment 2

[0064] Example 2 Cloning, selection and screening of llama V capable of neutralizing Lactococcus lactis phage P2 H H fragment

[0065] 2.1 Isolation of V of Lactococcus phage P2 H H fragment

[0066] Blood samples of approximately 200 ml were taken from llamas that were positive for phage P2 in the ELISA assay and centrifuged through a Ficoll (Pharmacia) step gradient to obtain an enriched lymphocyte population. Total RNA was isolated from these cells by guanidium extraction (for example as described by Chomczynnski and Sacchi (1987), Analytical Biochem., 162, 156-159). After the first cDNA was synthesized using MMLV-RT (Gibco-BRL) and random oligonucleotide primers (Pharmacia), the following specific primers were used to amplify the coding V H DNA fragments of the H segment and part of the long or short hinge region:

[0067] PstIv H -2B 5'-AGGTSMARCTGCAGSAGTCWGG-3' (SEQ.ID NO.4) s=c and G, M=A and c, R=A and G, W=A and T,

[0068] HindIIILa...

Embodiment 3

[0097] Example 3.V H H Fragment Neutralizes Efficacy of Lactococcus lactis Phage P2

[0098] 3.1 Production of V in Saccharomyces cerevisiae H Re-cloning in Episomal Plasmid System of H Fragment

[0099] V of VHH#1, VHH#2 and VHH#3 clones H The H-encoded genes were respectively derived from E. coli phagemid vectors pUR3827, pUR3828 and pUR3829 with PstI (present in V H The 5' end of the H gene and was introduced by primers VH-2B (SEQ.ID.NO.1)) and BstEII (naturally present in most V H H gene 3' end) and BstEII were digested and cloned into the episomal Saccharomyces cerevisiae secretory plasmid pUR4547, thus obtaining pUR3834, pUR3835 and pUR3836, respectively. The replication plasmid pUR4547 (accession number CBS100012) containing an Ori for autonomous replication in Saccharomyces cerevisiae can be produced through an inducible Ga17 promoter; -123) fused to V H The amino terminus of the H product completes the secretion. Yield was determined by Coomassie blue stained p...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

A method of inhibiting viral infection using a monovalent antigen binding protein comprising a single domain binding unit capable of binding to a virus is described. Preferably the protein is a heavy chain variable domain derived from an immunoglobulin naturally devoid of light chains. Food, pharmaceutical and cosmetic products comprising such proteins are also described together with a method for selecting inhibiting proteins from a large population of mainly containing non-inhibiting, but infectious agent binding fragments.

Description

field of invention [0001] The present invention relates to the use of antigen binding proteins in methods of inhibiting the infectivity of viruses or other infectious pathogens, products and compositions containing such proteins and methods of identifying and / or selecting antigen binding proteins having such activity. In particular, the present invention relates to a method of inhibiting viral infection using a monovalent antigen binding protein comprising a variable region derived from a heavy chain of an immunoglobulin lacking a light chain capable of binding to a virus . Background of the invention [0002] Antibodies are protein molecules that belong to a group of immunoglobulins produced by the immune system in response to antigens. The structure of most antibody molecules is based on a unit of four polypeptides containing two identical heavy chains and two identical light chains, covalently linked together by disulfide bonds. Each of the strands folds in discrete reg...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): A61K39/42A61P31/12C07K16/08C12N1/19C12N1/21C12N15/13C12N15/70C12N15/81G01N33/569G01N33/68
CPCC07K16/08A61K2039/505A61P31/12
Inventor S·贝泽默L·G·J·弗伦肯J·J·W·德哈尔德A·M·莱德波尔C·T·维尔里普斯
Owner UNILEVER NV