Characterization of epitopes of seminal plasma antigen stimulating human monoclonal sperm-immobilizing antibodies: a personal review

1989 ◽  
Vol 1 (3) ◽  
pp. 193 ◽  
Author(s):  
S Isojima
Keyword(s):  
Monoclonal Antibody ◽  
Recombinant Dna ◽  
Human Monoclonal Antibody ◽  
Human Sperm ◽  
Biologically Active ◽  
Blood Type ◽  
Type I ◽  
Recombinant Dna Technology ◽  
Sperm Binding ◽  
Carbohydrate Epitopes

In observations made between 1974 and 1984, 40 of 303 women with unexplained sterility (13.2%) showed positive sperm-immobilizing antibodies. Among many kinds of antibodies to human sperm including sperm coating antigens, the biologically active antibodies, such as sperm-immobilizing agglutinating antibodies and blocking antibodies for fertilization, could be relevant to infertility. Harmless sperm-binding antibodies are present even in the sera and cervical mucus of fertile women. Antigens corresponding to monoclonal antibodies (1C4, 2C6, 2E5), which were generated to human sperm coating antigens and indicated strong sperm-immobilizing activities, seemed to have carbohydrate epitopes. The majority of women with sterility of unknown cause appeared to raise sperm-immobilizing antibodies to carbohydrate epitopes of sperm. The stable human-mouse heterohybridoma H6-3C4 secreting monoclonal antibody (IgM, lambda) with extremely high titres of sperm-immobilizing (SI50, 5000 units) and agglutinating (1:1600) activities was successfully established from peripheral lymphocytes of a sterile woman. The chemical structure of an antigen epitope corresponding to human monoclonal antibody H6-3C4 was found to consist of internally repetitive, unbranched N-acetyllactosamine (blood type i antigen). Ejaculated human sperm appeared to be densely covered with sialyl blood type i antigen and sialyl branched internally repetitive N-acetyllactosamine (sialyl blood type I antigen). The antibody-producing V-H and V-L genes of the human hybridoma H6-3C1 were cloned and preserved to stabilize antibody production. Class-switch variants of heavy chain from mu to gamma (IgG1, lambda) in human Mab H6-3C4 were produced by recombinant DNA technology.

Molecular characterization of a human monoclonal antibody to B antigen in ABO blood type

2003 ◽  
Vol 86 (1) ◽  
pp. 45-51 ◽  
Author(s):  
Mika Kaneko ◽  
Yukinari Kato ◽  
Hidekazu Horiuchi ◽  
Motoki Osawa
Keyword(s):  
Monoclonal Antibody ◽  
Molecular Characterization ◽  
Human Monoclonal Antibody ◽  
Blood Type ◽  
Abo Blood Type

scholarly journals A Human monoclonal antibody targeting scavenger receptor class B type I precludes hepatitis C virus infection and viral spread in vitro and in vivo

Hepatology ◽  
2011 ◽  
Vol 55 (2) ◽  
pp. 364-372 ◽  
Author(s):  
Philip Meuleman ◽  
Maria Teresa Catanese ◽  
Lieven Verhoye ◽  
Isabelle Desombere ◽  
Ali Farhoudi ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Human Monoclonal Antibody ◽  
Scavenger Receptor ◽  
Type I ◽  
Hepatitis C Virus Infection ◽  
Viral Spread ◽  
Scavenger Receptor Class ◽  
Class B

scholarly journals Human sperm carbohydrate antigens defined by an antisperm human monoclonal antibody derived from an infertile woman bearing antisperm antibodies in her serum.

1988 ◽  
Vol 168 (1) ◽  
pp. 343-356 ◽  
Author(s):  
Y Tsuji ◽  
H Clausen ◽  
E Nudelman ◽  
T Kaizu ◽  
S Hakomori ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Human Monoclonal Antibody ◽  
Human Sperm ◽  
Infertile Woman ◽  
Antisperm Antibodies ◽  
Infertile Women ◽  
Epitope Structure ◽  
Sperm Immobilization ◽  
Sperm Antigen

The epitope structure of the human sperm antigen reacting with antibodies present in sera of infertile women has been studied using mAb H6-3C4, which produces immobilization of human sperm in the presence of complement. Another antibody, NUH2, which also induces human sperm immobilization, was used to substantiate the presence of a receptor on sperm involved in susceptibility to immobilization. Both antibodies defined type 2 chain polylactosamine structure. H6-3C4 is directed to internally located repetitive N-acetyllactosamine, i.e., sialyl-i, i, or fucosyl-i. NUH2 defines binary alpha 2----3 sialyl type 2 chain, i.e., sialyl-I. Thus, the presence of antibodies in the sera of infertile women directed to sperm lactosaminoglycan or lactosaminolipid could be the basis for infertility in these cases.

The Status of Acellular Pertussis Vaccines: Current Perspective

PEDIATRICS ◽  
1991 ◽  
Vol 88 (2) ◽  
pp. 401-405
Author(s):  
Keyword(s):  
United States ◽  
Pertussis Toxin ◽  
Recombinant Dna ◽  
The United States ◽  
Biologically Active ◽  
Current Status ◽  
Chemical Agent ◽  
Protein Antigens ◽  
Recombinant Dna Technology ◽  
Acellular Vaccines

Clinical studies of component ("acellular") pertussis vaccines have been undertaken in recent years, and several acellular vaccines have been used in Japan for 10 years. The Committee has reviewed these trials and related data and herein provides its assessment regarding the current status of the acellular vaccines and their possible use in the United States. The pertussis vaccines in current use in the United States are prepared from whole cells of a strain of Bordetella pertussis that is grown in broth medium, harvested by centrifugation, and killed or partially detoxified by heat or by the addition of a chemical agent, such as thimerosal, or by a combination of these methods. In contrast, the acellular vaccines developed in Japan and used in that country since 1981 contain one or more antigens derived from biologically active components of the B pertussis organism.1 An inactivated form of lymphocytosis promoting factor (LPF), also known as pertussis toxin and a variety of other synonyms, is a frequent component of acellular pertussis vaccines, as are filamentous hemagglutinins (FHA). Other constituents included in acellular vaccines are agglutinogens, a term denoting a variety of protein antigens on the surface of the B pertussis organism. Of the agglutinogens, a 69-kd outer membrane protein, when injected into neonatal mice, protects against B pertussis challenge.2 Acellular vaccines also have recently been derived from mutant pertussis toxin molecules prepared with recombinant DNA technology.3 The acellular vaccines produced in Japan have been classified into two types: B type, which contains LPF and FHA in roughly equal amounts; and T type, which contains mostly FHA but some LPF and agglutinogens.1,4

scholarly journals Recombinant human oviductin regulates protein tyrosine phosphorylation and acrosome reaction

Reproduction ◽  
2016 ◽  
Vol 152 (5) ◽  
pp. 561-573 ◽  
Author(s):  
Yuewen Zhao ◽  
Xiaojing Yang ◽  
Zongchao Jia ◽  
Robert L Reid ◽  
Pierre Leclerc ◽  
...  
Keyword(s):  
Tyrosine Phosphorylation ◽  
Recombinant Dna ◽  
Calcium Ionophore ◽  
Human Sperm ◽  
Early Embryo ◽  
Hek293 Cells ◽  
Spectrometric Analysis ◽  
Dependent Manner ◽  
Recombinant Dna Technology ◽  
Triton X

The mammalian oviduct synthesizes and secretes a major glycoprotein known as oviductin (OVGP1), which has been shown to interact with gametes and early embryos. Here we report the use of recombinant DNA technology to produce, for the first time, the secretory form of human OVGP1 in HEK293 cells. HEK293 colonies stably expressing recombinant human OVGP1 (rHuOVGP1) were established by transfecting cells with an expression vector pCMV6-Entry constructed with OVGP1 cDNA. Large quantities of rHuOVGP1 were obtained from the stably transfected cells using the CELLSPIN cell cultivation system. A two-step purification system was carried out to yield rHuOVGP1 with a purity of >95%. Upon gel electrophoresis, purified rHuOVGP1 showed a single band corresponding to the 120–150 kDa size range of human OVGP1. Mass spectrometric analysis of the purified rHuOVGP1 revealed its identity as human oviductin. Immunofluorescence showed the binding of rHuOVGP1 to different regions of human sperm cell surfaces in various degrees of intensity. Prior treatment of sperm with 1% Triton X-100 altered the immunostaining pattern of rHuOVGP1 with an intense immunostaining over the equatorial segment and post-acrosomal region as well as along the length of the tail. Addition of rHuOVGP1 in the capacitating medium further enhanced tyrosine phosphorylation of sperm proteins in a time-dependent manner. After 4-h incubation in the presence of rHuOVGP1, the number of acrosome-reacted sperm induced by calcium ionophore significantly increased. The successful production of rHuOVGP1 can now facilitate the study of the role of human OVGP1 in fertilization and early embryo development.

Recombinant Microorganisms as Tools for High Throughput Screening for Nonantibiotic Compounds

1997 ◽  
Vol 2 (1) ◽  
pp. 41-49 ◽  
Author(s):  
Ronald D. Klein ◽  
Timothy G. Geary
Keyword(s):  
High Throughput ◽  
High Throughput Screening ◽  
Heterologous Protein ◽  
Recombinant Dna ◽  
Biologically Active ◽  
Heterologous Proteins ◽  
Recombinant Dna Technology ◽  
Antibiotic Development ◽  
Recombinant Microorganisms

Microorganisms were among the first tools used for the discovery of biologically active compounds. Their utility reached a zenith during the era of antibiotic development in the 1950s and 1960s, then declined. Subsequently, a substantial role for microorganisms in the pharmaceutical industry developed with the realization that microbial fermentations were intriguing sources of nonantibiotic natural products. From recombinant DNA technology emerged another important role for microorganisms in pharmaceutical research: the expression of heterologous proteins for therapeutic products or for in vitro high throughput screens (HTSs). Recent developments in cloning, genetics, and expression systems have opened up new applications for recombinant microorganisms in screening for nonantibiotic compounds in HTSs. These screens employ microorganisms that depend upon the function of a heterologous protein for survival under defined nutritional conditions. Compounds that specifically target the heterologous protein can be identified by measuring viability of the microorganism under different nutrient selection. Advantages of this approach include a built-in selection for target selectivity, an easily measured end point that can be used for a multitude of different targets, and compatibility with automation required for HTSs. Mechanism-based HTSs using recombinant microorganisms can also address drug targets that are not readily approachable in other HTS formats, including certain enzymes; ion channels and transporters; and protein::protein, protein::DNA, and protein::RNA interactions.

Crystallization of the Fab from a human monoclonal antibody against gp 41 of human immunodeficiency virus type I

1990 ◽  
Vol 216 (3) ◽  
pp. 511-512 ◽  
Author(s):  
Elena Casale ◽  
Elisabeth Wenisch ◽  
Xiao-min He ◽  
Pier Giorgio Righetti ◽  
Robert S. Snyder ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Human Monoclonal Antibody ◽  
Type I ◽  
Immunodeficiency Virus

Characterization of a human monoclonal antibody obtained after immunization with plasma vaccine and a booster with recombinant-DNA hepatitis B vaccine

2002 ◽  
Vol 66 (3) ◽  
pp. 304-311 ◽  
Author(s):  
R.A. Heijtink ◽  
J. Kruining ◽  
P. van Bergen ◽  
S. de Rave ◽  
J. van Hattum ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Hepatitis B ◽  
Recombinant Dna ◽  
Human Monoclonal Antibody ◽  
Hepatitis B Vaccine
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