A Community Study of Antibodies among Individuals with Prior Lyme Disease in Endemic Areas.

The objective was to examine the prevalence of antibodies among symptomatic individuals with recent and past Lyme disease in endemic communities using standard assays and novel assays employing next-generation antigenic substrates. Single- and two-tiered algorithms included different anti- ELISAs and immunoblots. Antibody prevalence was examined in sera from 32 individuals with recent erythema migrans (EM), 335 individuals with persistent symptoms following treatment for Lyme disease (PTLS), and 41 community controls without a history of Lyme disease.

Comparative analysis of the infectivity rate of both Borrelia burgdorferi and Anaplasma phagocytophilum in humans and dogs in a New Jersey community.

Ticks are important vectors of disease and transmit an extensive array of bacterial, viral and protozoan diseases to both humans and dogs within a community. Borrelia burgdorferi, the causative agent of Lyme disease, has been extensively studied within both the human and veterinary population. Anaplasma phagocytophilum, an intracellular rickettsial pathogen also transmitted by ixodid ticks, has emerged as an important zoonotic infection with significant veterinary and medical implications, and is responsible for both canine granulocytic anaplasmosis and human granulocytic anaplasmosis.

A celiac cellular phenotype, with altered LPP sub-cellular distribution, is inducible in controls by the toxic gliadin peptide P31-43.

Celiac disease (CD) is a frequent inflammatory intestinal disease, with a genetic background, caused by gliadin-containing food. Undigested gliadin peptides P31-43 and P57-68 induce innate and adaptive T cell-mediated immune responses, respectively. Alterations in the cell shape and actin cytoskeleton are present in celiac enterocytes, and gliadin peptides induce actin rearrangements in both the CD mucosa and cell lines.

Enterocyte proliferation and signaling are constitutively altered in celiac disease.

Celiac disease (CD) occurs frequently, and is caused by ingestion of prolamins from cereals in subjects with a genetic predisposition. The small intestinal damage depends on an intestinal stress/innate immune response to certain gliadin peptides (e.g.

An undigested gliadin peptide activates innate immunity and proliferative signaling in enterocytes: the role in celiac disease.

Background: On ingestion of gliadin, the major protein component of wheat and other cereals, the celiac intestine is characterized by the proliferation of crypt enterocytes with an inversion of the differentiation/proliferation program. Gliadins and A-gliadin peptide P31-43, in particular, act as growth factors for crypt enterocytes in patients with celiac disease (CD). The effects of gliadin on crypt enterocyte proliferation and activation of innate immunity are mediated by epidermal growth factors (EGFs) and innate immunity mediators [interleukin 15 (IL15)].