Abstract: A conversion system for a gasoline engine based generator enables the use of heavier fuels. A vertically disposed vortex separation chamber includes an inlet proximate the bottom of the chamber and tangential to the longitudinal axis of the chamber for delivering to the chamber partially vaporized fuel in an air-fuel mixture from a carburetor associated with the engine. An outlet proximate the top of the chamber also tangential to the longitudinal axis of the chamber for delivering vaporized fuel from the chamber to the engine. An electric heater is in communication with the bottom of the chamber for heating the chamber wall to vaporize any fuel thereon so vaporized fuel is reintroduced in swirling air-fuel mixture in the chamber. A battery source charged by the generator provides power to the electric heater. A jacket is disposed about and spaced from the chamber wall creating an annulus between the jacket and the chamber wall.

Abstract: The present invention is directed to the cloning, sequencing, expression, and characterization of an immunoreactive ferric binding protein (Fbp) (38-kDa) protein of Ehrlichia canis encoded by a polynucleotide therefor. In particular embodiments, the protein is employed in an immunogenic composition, such as a vaccine. Methods to induce an immune reaction in an individual with compositions of the invention are provided.

Abstract: The present invention includes polypeptides, polynucleotides encoding the polypeptides, antibodies to the polypeptides, and methods for using the polypeptides and antibodies. The polypeptides include those with at least 80% identity to Rickettsia prowazekii TIyC or PId.

Abstract: Novel genes encoding homologous immunoreactive thio-disulfide oxidoreductases, or disulfide bond formation (Dsb) proteins from Ehrlichia chaffeensis and Ehrlichia canis are disclosed. While the E. chaffeensis and E. canis Dsb proteins are at most only 31% or less homologous to other known Dsb proteins, the Ehrlichia Dsbs contain a cysteine active site, Cys-Gly-Tyr-Cys, similar to those in known Dsb proteins. As predicted by 15-amino acid identical N-terminal signal peptides, the proteins are primarily localized in the periplasm of E. chaffeensis and E. canis, possibly playing a role in antigenicity and pathogenesis. The present invention provides the nucleotide and amino acid sequences and expression vectors for the E. chaffeensis and E. canis dsb genes, antisera directed against the proteins, and kits to determine whether an individual or animal is infected with a given species of Ehrlichia.

Abstract: The 28-kDa outer membrane proteins (P28) of Ehrlichia chaffeensis are encoded by a multigene family consisting of 21 members located in a 23-kb DNA fragment in the genome of E. chaffeensis. Fifteen of these proteins are claimed herein as novel sequences. The amino acid sequence identity of the various P28 proteins was 20-83%. Six of 10 tested p28 genes were actively transcribed in cell culture grown E. chaffeensis. RT-PCR also indicated that each of the p28 genes was monocistronic. These results suggest that the p28 genes are active genes and encode polymorphic forms of the P28 proteins. The P28s were also divergent among different isolates of E. chaffeensis. The large repertoire of the p28 genes in a single ehrlichial organism and antigenic diversity of the P28 among the isolates of E. chaffeensis suggest that the P28s may be involved in immune avoidance.

Abstract: Novel genes encoding homologous immunoreactive thio-disulfide oxidoreductases, or disulfide bond formation (Dsb) proteins from Ehrlichia chaffeensis and Ehrlichia canis are disclosed. While the E. chaffeensis and E. canis Dsb proteins are at most only 31% or less homologous to other known Dsb proteins, the Ehrlichia Dsbs contain a cysteine active site, Cys-Gly-Tyr-Cys, similar to those in known Dsb proteins. As predicted by 15-amino acid identical N-terminal signal peptides, the proteins are primarily localized in the periplasm of E. chaffeensis and E. canis, possibly playing a role in antigenicity and pathogenesis. The present invention provides the nucleotide and amino acid sequences and expression vectors for the E. chaffeensis and E. canis dsb genes, antisera directed against the proteins, and kits to determine whether an individual or animal is infected with a given species of Ehrlichia.

Abstract: The present invention is directed to the cloning, sequencing and expression of homologous immunoreactive 28-kDa protein genes, p28-1, -2, -3, -5, -6, -7, -9, from a polymorphic multiple gene family of Ehrlichia canis. Further disclosed is a multigene locus encoding all nine homologous 28-kDa protein genes of Ehrlichia canis. Recombinant Ehrlichia canis 28-kDa proteins react with convalescent phase antiserum from an E. canis-infected dog, and may be useful in the development of vaccines and serodiagnostics that are particularly effective for disease prevention and serodiagnosis.

Abstract: The 28-kDa outer membrane proteins (P28) of Ehrlichia chaffeensis are encoded by a multigene family consisting of 21 members located in a 23-kb DNA fragment in the genome of E. chaffeensis. Fifteen of these proteins are claimed herein as novel sequences. The amino acid sequence identity of the various P28 proteins was 20-83%. Six of 10 tested p28 genes were actively transcribed in cell culture grown E. chaffeensis. RT-PCR also indicated that each of the p28 genes was monocistronic. These results suggest that the p28 genes are active genes and encode polymorphic forms of the P28 proteins. The P28s were also divergent among different isolates of E. chaffeensis. The large repertoire of the p28 genes in a single ehrlichial organism and antigenic diversity of the P28 among the isolates of E. chaffeensis suggest that the P28s may be involved in immune avoidance.

Abstract: The present invention is directed to the cloning, sequencing and expression of homologous immunoreactive 28-kDa protein genes, p28-1, -2, -3, -5, -6, -7, -9, from a polymorphic multiple gene family of Ehrlichia canis. Further disclosed is a multigene locus encoding all nine homologous 28-kDa protein genes of Ehrlichia canis. Recombinant Ehrlichia canis 28-kDa proteins react with convalescent phase antiserum from an E. canis-infected dog, and may be useful in the development of vaccines and serodiagnostics that are particularly effective for disease prevention and serodiagnosis.

Abstract: Sequences encoding two immunoreactive glycoproteins were cloned from Ehrlichia canis (p153 gene) and Ehrlichia chaffeensis (p156 gene). These two glycoproteins are species-specific immunoreactive orthologs that are useful as subunit vaccines and for serologic and molecular diagnostics for E. canis and E. chaffeensis.

Abstract: The present invention is directed to the cloning, sequencing and expression of homologous immunoreactive 28-kDa protein genes, p28-1, -2, -3, -5, -6, -7, -9, from a polymorphic multiple gene family of Ehrlichia canis. Further disclosed is a multigene locus encoding all nine homologous 28-kDa protein genes of Ehrlichia canis. Recombinant Ehrlichia canis 28-kDa proteins react with convalescent phase antiserum from an E. canis-infected dog, and may be useful in the development of vaccines and serodiagnostics that are particularly effective for disease prevention and serodiagnosis.

Abstract: The present invention is directed to isolated nucleic acid molecules encoding Rickettsia felis outer membrane proteins (R. felis omp). Expression vectors and host cells comprising the nucleic acid molecules are also provided, as well as methods for increasing or decreasing the expression of R. felis omp in host cells. The invention further provides a method of screening a substance for the ability of the substance to modify R. felis omp function, and a method for isolating other R. felis omp molecules. DNA oligomers capable of hybridizing to the nucleic acid molecule encoding the R. felis omp are provided, which can be used to detect R. felis omp in a sample. An isolated R. felis omp is also provided. Antibodies specific for the protein, and fragments thereof, are provided, as are compositions comprising the protein and a compatible carrier. The subject invention further provides a method of preventing R. felis infections by R. felis present in a carrier host, and a method of reducing R.

Abstract: The present invention is directed to the cloning, sequencing and expression of homologous immunoreactive 28-kDa protein genes, p28-1, -2, -3, -5, -6, -7, -9, from a polymorphic multiple gene family of Ehrlichia canis. Further disclosed is a multigene locus encoding all nine homologous 28-kDa protein genes of Ehrlichia canis. Recombinant Ehrlichia canis 28-kDa proteins react with convalescent phase antiserum from an E. canis-infected dog, and may be useful in the development of vaccines and serodiagnostics that are particularly effective for disease prevention and serodiagnosis.

Abstract: Sequences encoding two immunoreactive glycoproteins were cloned from Ehrlichia canis (p153 gene) and Ehrlichia chaffeensis (p156 gene). These two glycoproteins are species-specific immunoreactive orthologs that are useful as subunit vaccines and for serologic and molecular diagnostics for E. canis and E. chaffeensis.

Abstract: The present invention is directed to the cloning, sequencing and expression of homologous immunoreactive 28-kDa protein genes, p28-1, -2, -3, -5, -6, -7, -9, from a polymorphic multiple gene family of Ehrlichia canis. Further disclosed is a multigene locus encoding all nine homologous 28-kDa protein genes of Ehrlichia canis. Recombinant Ehrlichia canis 28-kDa proteins react with convalescent phase antiserum from an E. canis-infected dog, and may be useful in the development of vaccines and serodiagnostics that are particularly effective for disease prevention and serodiagnosis.

Abstract: A filter system including a housing with an intake and an outlet, a pleated carbon filter disposed between the intake and the outlet for filtering out vapors entering the intake, and a hydrophobic solution dispersed about the pleated carbon filter to inhibit adsorption of water thereby increasing the adsorption capacity of the pleated carbon filter especially in high relative humidity environments. The hydrophobic solution is selected so that it does not decrease the adsorption capacity of the carbon filter. Also disclosed is a method of making such a filter.

Abstract: The present invention is directed to the cloning, sequencing and expression of homologous immunoreactive 28-kDa protein genes, p28-1, -2, -3, -5, -6, -7, -9, from a polymorphic multiple gene family of Ehrlichia canis. Further disclosed is a multigene locus encoding all nine homologous 28-kDa protein genes of Ehrlichia canis. Recombinant Ehrlichia canis 28-kDa proteins react with convalescent phase antiserum from an E. canis-infected dog, and may be useful in the development of vaccines and serodiagnostics that are particularly effective for disease prevention and serodiagnosis.

Abstract: The 28-kDa outer membrane proteins (P28) of Ehrlichia chaffeensis are encoded by a multigene family consisting of 21 members located in a 23-kb DNA fragment in the genome of E. chaffeensis. Fifteen of these proteins are claimed herein as novel sequences. The amino acid sequence identity of the various P28 proteins was 20-83%. Six of 10 tested p28 genes were actively transcribed in cell culture grown E. chaffeensis. RT-PCR also indicated that each of the p28 genes was monocistronic. These results suggest that the p28 genes are active genes and encode polymorphic forms of the P28 proteins. The P28s were also divergent among different isolates of E. chaffeensis. The large repertoire of the p28 genes in a single ehrlichial organism and antigenic diversity of the P28 among the isolates of E. chaffeensis suggest that the P28s may be involved in immune avoidance.

Abstract: The 28-kDa outer membrane proteins (P28) of Ehrlichia chaffeensis are encoded by a multigene family consisting of 21 members located in a 23-kb DNA fragment in the genome of E. chaffeensis. Fifteen of these proteins are claimed herein as novel sequences. The amino acid sequence identity of the various P28 proteins was 20-83%. Six of 10 tested p28 genes were actively transcribed in cell culture grown E. chaffeensis. RT-PCR also indicated that each of the p28 genes was monocistronic. These results suggest that the p28 genes are active genes and encode polymorphic forms of the P28 proteins. The P28s were also divergent among different isolates of E. chaffeensis. The large repertoire of the p28 genes in a single ehrlichial organism and antigenic diversity of the P28 among the isolates of E. chaffeensis suggest that the P28s may be involved in immune avoidance.

Abstract: The present invention is directed to the cloning, sequencing and expression of homologous immunoreactive 28-kDa protein genes, p28-1, -2, -3, -5, -6, -7, -9, from a polymorphic multiple gene family of Ehrlichia canis. Further disclosed is a multigene locus encoding all nine homologous 28-kDa protein genes of Ehrlichia canis. Recombinant Ehrlichia canis 28-kDa proteins react with convalescent phase antiserum from an E. canis-infected dog, and may be useful in the development of vaccines and serodiagnostics that are particularly effective for disease prevention and serodiagnosis.