Compounds > 1-oleoyl-2-stearoylphosphatidylcholine

1-oleoyl-2-stearoylphosphatidylcholine and Lyme-Disease

1-oleoyl-2-stearoylphosphatidylcholine has been researched along with Lyme-Disease* in 2 studies

Other Studies

2 other study(ies) available for 1-oleoyl-2-stearoylphosphatidylcholine and Lyme-Disease

Article	Year
Development of an OspC-based tetravalent, recombinant, chimeric vaccinogen that elicits bactericidal antibody against diverse Lyme disease spirochete strains. Vaccine, 2007, Jan-05, Volume: 25, Issue:3 Lyme disease is the most common arthropod-borne disease in North America and Europe. At present, there is no commercially available vaccine for use in humans. Outer surface protein C (OspC) has antigenic and expression characteristics that make it an attractive vaccine candidate; however, sequence heterogeneity has impeded its use as a vaccinogen. Sequence analyses have identified 21 well defined OspC phyletic groups or "types" (designated A-U). In this report we have mapped the linear epitopes presented by OspC types B, K, and D during human and murine infection and exploited these epitopes (along with the previously identified type A OspC linear epitopes) in the development of a recombinant, tetravalent, chimeric vaccinogen. The construct was found to be highly immunogenic in mice and the induced antibodies surface labeled in vitro cultivated spirochetes. Importantly, vaccination induced complement-dependent bactericidal antibodies against strains expressing each of the OspC types that were incorporated into the construct. These results suggest that an effective and broadly protective polyvalent OspC-based Lyme disease vaccine can be produced as a recombinant, chimeric protein. Topics: Amino Acid Sequence; Animals; Base Sequence; Borrelia burgdorferi; Cloning, Molecular; Enzyme-Linked Immunosorbent Assay; Epitopes; Fluorescent Antibody Technique; Immunoblotting; Lyme Disease; Lyme Disease Vaccines; Male; Mice; Mice, Inbred C3H; Models, Molecular; Molecular Sequence Data; Phosphatidylcholines; Reverse Transcriptase Polymerase Chain Reaction; Species Specificity; Vaccines, Synthetic	2007
Peptide-based OspC enzyme-linked immunosorbent assay for serodiagnosis of Lyme borreliosis. Journal of clinical microbiology, 1998, Volume: 36, Issue:12 Sera from 210 patients with Lyme borreliosis (LB) were studied by an enzyme-linked immunosorbent assay (ELISA) based on a synthetic peptide (pepC10) comprising the C-terminal 10-amino-acid residues of OspC of Borrelia burgdorferi. We found that 36.3 and 45.0% of the serum samples from patients with erythema migrans (EM) and neuroborreliosis (NB), respectively, displayed immunoglobulin M (IgM) anti-pepC10 reactivities, while these samples rarely ( Topics: Adolescent; Adult; Aged; Aged, 80 and over; Antibodies, Bacterial; Borrelia burgdorferi Group; Child; Enzyme-Linked Immunosorbent Assay; Female; Humans; Immunoglobulin G; Immunoglobulin M; Lyme Disease; Male; Middle Aged; Peptide Fragments; Phosphatidylcholines; Serologic Tests	1998

Article

Year

Development of an OspC-based tetravalent, recombinant, chimeric vaccinogen that elicits bactericidal antibody against diverse Lyme disease spirochete strains.

Vaccine, 2007, Jan-05, Volume: 25, Issue:3

Lyme disease is the most common arthropod-borne disease in North America and Europe. At present, there is no commercially available vaccine for use in humans. Outer surface protein C (OspC) has antigenic and expression characteristics that make it an attractive vaccine candidate; however, sequence heterogeneity has impeded its use as a vaccinogen. Sequence analyses have identified 21 well defined OspC phyletic groups or "types" (designated A-U). In this report we have mapped the linear epitopes presented by OspC types B, K, and D during human and murine infection and exploited these epitopes (along with the previously identified type A OspC linear epitopes) in the development of a recombinant, tetravalent, chimeric vaccinogen. The construct was found to be highly immunogenic in mice and the induced antibodies surface labeled in vitro cultivated spirochetes. Importantly, vaccination induced complement-dependent bactericidal antibodies against strains expressing each of the OspC types that were incorporated into the construct. These results suggest that an effective and broadly protective polyvalent OspC-based Lyme disease vaccine can be produced as a recombinant, chimeric protein.

Topics: Amino Acid Sequence; Animals; Base Sequence; Borrelia burgdorferi; Cloning, Molecular; Enzyme-Linked Immunosorbent Assay; Epitopes; Fluorescent Antibody Technique; Immunoblotting; Lyme Disease; Lyme Disease Vaccines; Male; Mice; Mice, Inbred C3H; Models, Molecular; Molecular Sequence Data; Phosphatidylcholines; Reverse Transcriptase Polymerase Chain Reaction; Species Specificity; Vaccines, Synthetic

2007

Peptide-based OspC enzyme-linked immunosorbent assay for serodiagnosis of Lyme borreliosis.

Journal of clinical microbiology, 1998, Volume: 36, Issue:12

Sera from 210 patients with Lyme borreliosis (LB) were studied by an enzyme-linked immunosorbent assay (ELISA) based on a synthetic peptide (pepC10) comprising the C-terminal 10-amino-acid residues of OspC of Borrelia burgdorferi. We found that 36.3 and 45.0% of the serum samples from patients with erythema migrans (EM) and neuroborreliosis (NB), respectively, displayed immunoglobulin M (IgM) anti-pepC10 reactivities, while these samples rarely (

Topics: Adolescent; Adult; Aged; Aged, 80 and over; Antibodies, Bacterial; Borrelia burgdorferi Group; Child; Enzyme-Linked Immunosorbent Assay; Female; Humans; Immunoglobulin G; Immunoglobulin M; Lyme Disease; Male; Middle Aged; Peptide Fragments; Phosphatidylcholines; Serologic Tests

1998