VlsE Protein of Borrelia burgdorferi

Catalog Number:
BB-VISE-005P
Price: $249.00
Detailed Description

BB-VISE-005P

Name

Recombinant VlsE protein of Borrelia burgdorferi

Description

N-terminal 6x His tagged VlsE protein (GenBank accession# U76405) of Borrelia burgdorferi that is associated with the Lyme disease borreliosis.

Source

Recombinant protein expressed and purified from HEK293 cells

Application

Western Blot, antigen, ELISA, etc.

Purity

> 95% (by SDS-PAGE)

Endotoxin

<0.01 EU per µg of purified protein by LAL test

Size

50 µg

For Downloading

==>> DATA SHEET

Other Names: VlsE, Variable Major Protein-Like Sequence Expressed, Variable Surface Antigen VlsE, VlsE Lipoprotein, Lyme Disease Variable Surface Antigen, Variable Lipoprotein-Like Sequence Protein E.

About Borrelia burgdorferi VlsE Protein

Variable Major Protein-Like Sequence Expressed (VlsE) is a surface-exposed lipoprotein encoded by the vlsE gene of Borrelia burgdorferi, the causative agent of Lyme disease. VlsE is one of the most important virulence factors of the Lyme disease spirochete and plays a central role in immune evasion and persistent infection within mammalian hosts. The protein is expressed on the bacterial outer membrane and undergoes continuous antigenic variation through segmental gene conversion events involving multiple silent vls cassettes, generating extensive sequence diversity during infection. This antigenic variation allows B. burgdorferi to evade host antibody responses and establish long-term persistence in infected tissues.

Structurally, VlsE is a highly immunogenic surface lipoprotein containing conserved and variable regions. The variable surface loops are exposed on the outer surface of the bacterium and undergo continual sequence changes, while conserved regions remain largely protected from immune recognition. This unique structural organization enables VlsE to shield critical epitopes from antibody binding and contributes significantly to the pathogen's ability to avoid immune clearance.

Because VlsE is strongly expressed during mammalian infection and elicits robust antibody responses, it has become one of the most widely utilized antigens for Lyme disease serological testing. Recombinant VlsE and its conserved IR6-derived C6 peptide are commonly incorporated into diagnostic assays for the detection of Lyme disease antibodies. In addition, VlsE serves as an important research tool for studying host-pathogen interactions, antigenic variation mechanisms, immune evasion strategies, and vaccine development efforts targeting Borrelia burgdorferi.

eEnzyme's Recombinant Borrelia burgdorferi VlsE Protein is expressed in HEK293 cells and purified to high purity. The recombinant protein is suitable for antibody production, ELISA development, serological assay validation, antigenicity studies, and Lyme disease research applications.

Applications of Borrelia burgdorferi VlsE Protein

• Lyme disease diagnostic assay development
• ELISA and serological testing applications
• Antibody generation and characterization
• Antigenicity and epitope mapping studies
• Host-pathogen interaction research
• Immune evasion mechanism investigations
• Vaccine and therapeutic development research
• Western blot and immunoassay applications

Biological Significance of VlsE

VlsE is a critical virulence factor that enables Borrelia burgdorferi to persist within mammalian hosts despite the development of adaptive immune responses. Through continuous antigenic variation, VlsE generates an evolving repertoire of surface epitopes that prevents effective antibody-mediated clearance. This mechanism is essential for long-term infection and contributes significantly to the chronic nature of Lyme disease. Studies have demonstrated that VlsE expression is tightly regulated during mammalian infection and is required for efficient immune evasion and persistence in immunocompetent hosts.

In addition to its role in pathogenesis, VlsE is one of the most diagnostically important antigens of B. burgdorferi. Antibodies directed against VlsE are generated early and persist throughout infection, making the protein a valuable biomarker for Lyme disease diagnosis. Structural studies have further demonstrated that the highly variable surface loops of VlsE help shield conserved protein regions from antibody recognition, providing a sophisticated mechanism for immune escape. Because of its central role in bacterial survival, pathogenesis, and clinical diagnosis, VlsE remains one of the most extensively studied proteins in Lyme disease research.

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