scholarly journals Lyme Disease Pathogenesis

2022 ◽  
pp. 473-518
Author(s):  
Jenifer Coburn ◽  
Brandon Garcia ◽  
Linden T. Hu ◽  
Mollie W. Jewett ◽  
Peter Kraiczy ◽  
...  
Keyword(s):  
Lyme Disease ◽  
Disease Pathogenesis

scholarly journals Lyme Disease Pathogenesis

2021 ◽  
Author(s):  
Jenifer Coburn ◽  
Brandon Garcia ◽  
Linden T. Hu ◽  
Mollie W. Jewett ◽  
Peter Kraiczy ◽  
...  
Keyword(s):  
Lyme Disease ◽  
Disease Pathogenesis

Chemokines and Toll-like receptors in Lyme disease pathogenesis

2005 ◽  
Vol 11 (3) ◽  
pp. 114-120 ◽  
Author(s):  
Mireia Guerau-de-Arellano ◽  
Brigitte T. Huber
Keyword(s):  
Lyme Disease ◽  
Toll Like Receptors ◽  
Disease Pathogenesis

Animal models of Lyme disease: pathogenesis and immunoprophylaxis

1994 ◽  
Vol 2 (11) ◽  
pp. 431-437 ◽  
Author(s):  
Mario T. Philipp ◽  
Barbara J.B. Johnson
Keyword(s):  
Animal Models ◽  
Lyme Disease ◽  
Disease Pathogenesis

Lyme disease: Pathogenesis and vaccine development

1999 ◽  
Vol 289 (5-7) ◽  
pp. 690-695 ◽  
Author(s):  
Markus M. Simon ◽  
Yvonne Bauer ◽  
Weimin Zhong ◽  
Heidelore Hofmann ◽  
Reinhard Wallich
Keyword(s):  
Lyme Disease ◽  
Vaccine Development ◽  
Disease Pathogenesis

scholarly journals Selective Binding of Borrelia burgdorferi OspE Paralogs to Factor H and Serum Proteins from Diverse Animals: Possible Expansion of the Role of OspE in Lyme Disease Pathogenesis

2006 ◽  
Vol 74 (3) ◽  
pp. 1967-1972 ◽  
Author(s):  
Kelley M. Hovis ◽  
Emily Tran ◽  
Christina M. Sundy ◽  
Eric Buckles ◽  
John V. McDowell ◽  
...  
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Host Range ◽  
Serum Proteins ◽  
Factor H ◽  
Disease Pathogenesis ◽  
Selective Binding

ABSTRACT The binding of Borrelia burgdorferi OspE, OspF, and family 163 (Elp) proteins to factor H/factor H-like protein 1 (FHL-1) and other serum proteins from different animals was assessed. OspE paralogs bound factor H and unidentified serum proteins from a subset of animals, while OspF and Elp proteins did not. These data advance our understanding of factor H binding, the host range of the Lyme spirochetes, and the expanding role of OspE in pathogenesis.

New ultrastructural findings about Borrelia burgdorferi by cryofixation, negative staining, thin sectioning and scanning techniques

1990 ◽  
Vol 48 (3) ◽  
pp. 582-583
Author(s):  
S. F. Hayes ◽  
M. D. Corwin ◽  
T. G. Schwan ◽  
D. W. Dorward ◽  
W. Burgdorfer
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Structural Characterization ◽  
Negative Staining ◽  
Low Speed ◽  
Thin Sectioning ◽  
Ultrastructural Findings

Characterization of Borrelia burgdorferi strains by means of negative staining EM has become an integral part of many studies related to the biology of the Lyme disease organism. However, relying solely upon negative staining to compare new isolates with prototype B31 or other borreliae is often unsatisfactory. To obtain more satisfactory results, we have relied upon a correlative approach encompassing a variety EM techniques, i.e., scanning for topographical features and cryotomy, negative staining and thin sectioning to provide a more complete structural characterization of B. burgdorferi.For characterization, isolates of B. burgdorferi were cultured in BSK II media from which they were removed by low speed centrifugation. The sedimented borrelia were carefully resuspended in stabilizing buffer so as to preserve their features for scanning and negative staining. Alternatively, others were prepared for conventional thin sectioning and for cryotomy using modified procedures. For thin sectioning, the fixative described by Ito, et al.

Insights into amyloid disease from fly models

2014 ◽  
Vol 56 ◽  
pp. 69-83 ◽  
Author(s):  
Ko-Fan Chen ◽  
Damian C. Crowther
Keyword(s):  
Drosophila Melanogaster ◽  
Neurodegenerative Disorders ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Disease Pathogenesis ◽  
Amyloid Aggregates ◽  
Aβ Amyloid ◽  
Polypeptide Chains ◽  
Amyloid Diseases

The formation of amyloid aggregates is a feature of most, if not all, polypeptide chains. In vivo modelling of this process has been undertaken in the fruitfly Drosophila melanogaster with remarkable success. Models of both neurological and systemic amyloid diseases have been generated and have informed our understanding of disease pathogenesis in two main ways. First, the toxic amyloid species have been at least partially characterized, for example in the case of the Aβ (amyloid β-peptide) associated with Alzheimer's disease. Secondly, the genetic underpinning of model disease-linked phenotypes has been characterized for a number of neurodegenerative disorders. The current challenge is to integrate our understanding of disease-linked processes in the fly with our growing knowledge of human disease, for the benefit of patients.

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