Outer Surface Protein A
Outer Surface Protein A - Related Videos
09:55
From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
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Cited by 8 •
2016
β-barrel outer membrane proteins (OMPs) serve many functions within the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. Here, we hope to alleviate a known bottleneck in structural studies by presenting protocols for the production of β-barrel OMPs in sufficient quantities for structure determination by X-ray crystallography or NMR spectroscopy.
01:11
Protein Transport to the Outer Chloroplast Membrane
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2023
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation. Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
10:47
Immuno-fluorescence Assay of Leptospiral Surface-exposed Proteins
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Cited by 23 •
2011
An efficient method to assess surface-exposure of leptospiral proteins is described. The method is specifically designed to avoid disruption of the fragile outer membrane of leptospiral cells. This technique requires employment of several negative controls to assess the integrity of the outer membrane and specificity of antibody reaction.
10:21
Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
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Cited by 12 •
2016
A protocol for the production, purification, and use of enzyme packaged outer membrane vesicles (OMV) providing for enhanced enzyme stability for implementation across diverse applications is presented.
10:35
Surface Passivation for Single-molecule Protein Studies
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Cited by 270 •
2014
We describe a method for passivating a glass surface using polyethylene glycol (PEG). This protocol covers surface cleaning, surface functionalization, and PEG coating. We introduce a new strategy for treating the surface with PEG molecules over two rounds, which yields superior quality of passivation compared to existing methods.
FAQs
Its expression changes according to whether Borrelia is in the tick midgut or entering a mammalian host during feeding. This regulated pattern links protein production to environmental conditions and transmission stages, allowing researchers to examine how the bacterium adapts as it moves between hosts. The contrast also helps distinguish persistence in the vector from behavior during mammalian infection.
Within the tick midgut, OspA supports Borrelia persistence before transmission. Its reduced expression during movement into a mammalian host indicates that the protein’s importance is associated with the vector stage rather than being constant throughout the bacterium’s cycle. Studying this shift helps clarify how bacterial surface components respond to changing host and vector environments.
Antibodies against OspA can target Borrelia while the bacterium remains inside the tick. This makes antibody recognition relevant to transmission biology, because the immune response can act against the bacterial stage present in the vector rather than only after entry into a mammalian host. OspA therefore connects molecular recognition with a specific point in the transmission cycle.
A useful comparison examines OspA expression in Borrelia residing in the tick midgut and during the bacterium’s entry into a mammalian host as the tick feeds. The expected difference is higher expression in the midgut and reduced expression during host entry. This comparison can support studies of stage-specific regulation, bacterial adaptation, and host-vector interactions.
OspA has served as a model antigen because antibodies directed against it can target Borrelia within the tick. Vaccine studies can therefore evaluate whether immune recognition interferes with the bacterial stage associated with persistence in the vector and transmission. Its stage-specific expression provides a focused context for investigating how vaccination might affect the host-vector phase of Lyme disease.
OspA studies can connect several biological questions: how Borrelia persists in a tick, how its surface composition changes during feeding, how bacterial adaptation supports movement between hosts, and how antibodies recognize the organism. Together, these questions place the protein within a broader framework for analyzing Lyme disease transmission and interactions among the bacterium, tick, and mammalian host.