Expression of meningococcal epitopes in LamB of Escherichia coli and the stimulation of serosubtype-specific antibody responses

1993 ◽  
Vol 10 (1) ◽  
pp. 203-213 ◽  
Author(s):  
J. McCarvil ◽  
A. J. McKenna ◽  
C. Grief ◽  
C. S. Hoy ◽  
D. Sesardic ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Specific Antibody ◽  
Antibody Responses ◽  
Stimulation Of

scholarly journals Species-Specific Antibody Responses to the Recombinant 53-Kilodalton Excretory and Secretory Proteins in Mice Infected with Trichinella spp.

2008 ◽  
Vol 15 (3) ◽  
pp. 468-473 ◽  
Author(s):  
Isao Nagano ◽  
Zhiliang Wu ◽  
Yuzo Takahashi
Keyword(s):  
Escherichia Coli ◽  
Recombinant Protein ◽  
Recombinant Proteins ◽  
Specific Antibody ◽  
Expression System ◽  
Amino Acid Sequences ◽  
Antibody Responses ◽  
Secretory Proteins ◽  
Muscle Larvae ◽  
Species Specific

ABSTRACT The 53-kDa proteins in larval excretory and secretory (E-S) products were expressed from five Trichinella species (T. spiralis, T. britovi, T. nativa, T. pseudospiralis, and T. papuae), using the Escherichia coli expression system, and the antibody responses to the 53-kDa recombinant proteins in mice infected with Trichinella spp. were analyzed by Western blotting. The 53-kDa protein is conserved among the five Trichinella species, with >60% similarity in amino acid sequences. The 53-kDa recombinant proteins of T. spiralis and T. pseudospiralis reacted to sera from mice infected with T. spiralis and T. pseudospiralis at 8 days postinfection (p.i.), respectively. An antibody against the 53-kDa recombinant protein of T. spiralis recognized the 53-kDa protein in the crude extracts from adult worms and 30-day p.i. muscle larvae and E-S products from muscle larvae of T. spiralis but did not recognize any proteins from T. pseudospiralis. The sera from the mice infected with T. spiralis strongly reacted with the 53-kDa recombinant protein of T. spiralis but did not react with the 53-kDa recombinant proteins of T. britovi, T. nativa, T. pseudospiralis, and T. papuae. Similarly, the sera from mice infected with T. britovi, T. nativa, T. pseudospiralis, or T. papuae strongly reacted with the 53-kDa recombinant proteins of T. britovi, T. nativa, T. pseudospiralis, or T. papuae, respectively. These results showed that the 53-kDa recombinant proteins provide early and species-specific antibody responses in mice infected with Trichinella spp.

scholarly journals Construction and evaluation of a chimeric protein made fromFasciola hepaticaleucine aminopeptidase and cathepsin L1

2014 ◽  
Vol 90 (1) ◽  
pp. 7-13 ◽  
Author(s):  
K. Hernández-Guzmán ◽  
A. Sahagún-Ruiz ◽  
A.J. Vallecillo ◽  
I. Cruz-Mendoza ◽  
H. Quiroz-Romero
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Western Blot ◽  
Specific Antibody ◽  
Diagnostic Tool ◽  
Leucine Aminopeptidase ◽  
Fasciola Hepatica ◽  
Chimeric Protein ◽  
Antibody Responses ◽  
Immunogenic Properties

AbstractLeucine aminopeptidase (LAP) and cathepsin L1 (CL1) are important enzymes for the pathogenesis and physiology ofFasciola hepatica. These enzymes were analysedin silicoto design a chimeric protein containing the most antigenic sequences of LAP (GenBank; AAV59016.1; amino acids 192–281) and CL1 (GenBank CAC12806.1; amino acids 173–309). The cloned 681-bp chimeric fragment (rFhLAP-CL1) contains 270 bp from LAP and 411 bp from CL1, comprising three epitopes, DGRVVHLKY (amino acids 54–62) from LAP, VTGYYTVHSGSEVELKNLV (amino acids 119–137) and YQSQTCLPF (amino acids 161–169) from CL1. The ~25 kDa rFhLAP-CL1 chimeric protein was expressed from the pET15b plasmid in the Rosetta (DE3)Escherichia colistrain. The chimeric protein rFhLAP-CL1, which showed antigenic and immunogenic properties, was recognized in Western blot assays usingF. hepatica-positive bovine sera, and induced strong, specific antibody responses following immunization in rabbits. The newly generated chimeric protein may be used as a diagnostic tool for detection of antibodies againstF. hepaticain bovine sera and as an immunogen to induce protection against bovine fasciolosis.

scholarly journals Association of Escherichia coli J5-Specific Serum Antibody Responses with Clinical Mastitis Outcome for J5 Vaccinate and Control Dairy Cattle

2008 ◽  
Vol 16 (2) ◽  
pp. 209-217 ◽  
Author(s):  
David J. Wilson ◽  
Bonnie A. Mallard ◽  
Jeanne L. Burton ◽  
Ynte H. Schukken ◽  
Yrjo T. Grohn
Keyword(s):  
Escherichia Coli ◽  
Dairy Cattle ◽  
Milk Production ◽  
Specific Antibody ◽  
Serum Antibody ◽  
Clinical Mastitis ◽  
Immunoglobulin M ◽  
Antibody Responses ◽  
Enzyme Linked Immunosorbent Assay ◽  
And Control

ABSTRACT Dairy cattle in two commercial Holstein herds were randomly selected to be vaccinated twice with J5, at approximately 60 days and 28 days before the expected calving date, or to be untreated controls. Based on whether milk production changed following clinical mastitis or whether cows were culled or died within 30 days after onset, 51 mastitis cases were classified as severe or mild. J5-specific antibody responses were evaluated by enzyme-linked immunosorbent assay of all 32 severe and 19 mild cases. The amounts of J5-specific immunoglobulin M (IgM), IgG1, and IgG2 antibodies in sera from the 27 J5 vaccinates were compared with those of the 24 controls. At drying off (before J5 vaccination), all cows had similar amounts of J5-specific antibody. Immediately after calving (approximately 28 days after the second vaccination), J5 vaccinates had significantly higher production of J5-specific IgG1 and IgG2 than controls. When cows were tested following clinical mastitis, none of the three antibody classes differed significantly between the controls and the vaccinates. Vaccinates that contracted Escherichia coli mastitis had 75% less milk loss than controls. The cows that contracted clinical mastitis later in lactation, the unvaccinated controls, and those infected with E. coli had more milk loss following mastitis. The hazards of being culled for all reasons and of being culled for mastitis were significantly lower for J5 vaccinates. Vaccination with J5 was associated with protection against milk production loss and culling following clinical mastitis, and it was also significantly associated with changes in J5-specific IgM, IgG1, and IgG2 antibodies in sera of vaccinated cows.

scholarly journals Biofilm Lithography enables high-resolution cell patterning via optogenetic adhesin expression

2018 ◽  
Vol 115 (14) ◽  
pp. 3698-3703 ◽  
Author(s):  
Xiaofan Jin ◽  
Ingmar H. Riedel-Kruse
Keyword(s):  
Escherichia Coli ◽  
Cell Patterning ◽  
Biophysical Model ◽  
Microbial Consortia ◽  
Bacterial Biofilms ◽  
Surface Pretreatment ◽  
Resolution Cell ◽  
Stimulation Of

Bacterial biofilms represent a promising opportunity for engineering of microbial communities. However, our ability to control spatial structure in biofilms remains limited. Here we engineerEscherichia coliwith a light-activated transcriptional promoter (pDawn) to optically regulate expression of an adhesin gene (Ag43). When illuminated with patterned blue light, long-term viable biofilms with spatial resolution down to 25 μm can be formed on a variety of substrates and inside enclosed culture chambers without the need for surface pretreatment. A biophysical model suggests that the patterning mechanism involves stimulation of transiently surface-adsorbed cells, lending evidence to a previously proposed role of adhesin expression during natural biofilm maturation. Overall, this tool—termed “Biofilm Lithography”—has distinct advantages over existing cell-depositing/patterning methods and provides the ability to grow structured biofilms, with applications toward an improved understanding of natural biofilm communities, as well as the engineering of living biomaterials and bottom–up approaches to microbial consortia design.

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