Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “LEPTOSPIRA”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 649 records · Page 36Linked to original sources
PubMed1988

Restriction endonuclease DNA analysis of Leptospira interrogans serovars Icterohaemorrhagiae and Copenhageni.

Leptospira interrogans serovar icterohaemorrhagiae strains Ictero No. I and RGA and serovar copenhageni strains M20, Shiromizu and Shibaura were examined by restriction endonuclease DNA analysis. Fifteen endonucleases (AluI, BamHI, BglII, EcoRI, HaeIII, HhaI, HindIII, KpnI, PstI, SacI, SalI, SmaI, StyI, XbaI and XhoI) were used as the digesting enzymes. Strain Ictero No. I showed endonuclease cleavage patterns which differed from those of the other four strains only when it was digested with enzymes KpnI and HindIII. When digested with KpnI, an extra band of about 5.4 kb was clearly produced, and when digested with HindIII, an extra band of about 25 kb was produced. When the other 13 enzymes were used, no differences were found between the endonuclease cleavage patterns among the five strains. Moreover, strains RGA, M20, Shiromizu and Shibaura could not be distinguished by the restriction endonuclease DNA analysis using all 15 endonucleases. In addition, six newly isolated leptospires from patients with leptospirosis and from Rattus norvegicus were compared with the Ictero No. I and M20 strains, by restriction endonuclease DNA analysis using enzymes KpnI and HindIII. Three leptospires belonging to serovar icterohaemorrhagiae showed the same endonuclease cleavage patterns as the M20 strain. The other three strains, which belong to serovar copenhageni, showed almost the same endonuclease cleavage patterns as the M20 strain; only the Kai ima 702 strain produced an extra band which was not identical to the Ictero No. I-specific extra band when digested with HindIII. The leptospiral restriction endonuclease DNA analysis has revealed taxonomic structures that are unrecognized by serology alone.

Animals↗
PubMed1988

Expression of antigen genes of Leptospira interrogans serovar canicola in Escherichia coli.

Leptospira interrogans serovar canicola DNA was cloned into the plasmid pBR322 and introduced into E. coli. Eight out of approximately 10,000 transformants were found to express antigens of canicola by ELISA including colony ELISA blot test using anti-canicola antiserum. The canicola antigens expressed in the transformants reacted with the antisera against the serovars belonging to Canicola serogroup and other serogroups of L. interrogans. They did not react, however, with the antiserum against L. biflexa (with only one exception) nor with the antiserum against Leptonema illini. Thus, the recombinant DNA technique may provide alternative possibilities for preparing antigens of leptospires.

Antigens, Bacterial↗
PubMed1991

Comparison of protective effects with tetra-valent glycolipid antigens and whole cell-inactivated vaccine in experimental infection of Leptospira.

The protective antigens (PAgs), glycolipid substance, were extracted from Leptospira interrogans serovars autumnalis, hebdomadis, australis and copenhageni, which were considered as main causal serovars of human leptospirosis in Japan, with chloroform-methanol-water (1:2:0.8, [vol/vol/vol]) solution. The tetra-valent formalin-inactivated leptospiral vaccine (Weil's disease and Akiyami combined vaccine) composed of the four serovars mentioned are used as vaccine to protect human from leptospiral infection in Japan. The protective effect, agglutinating antibody-inducing activity and opsonin-inducing activity of tetra-valent PAgs were compared with those of vaccines now in use, which were supplied by two companies, Takeda Chemical Industries, Ltd., and Denka-Seiken Co., in Japan. The tetra-valent PAgs which contained 10 micrograms of each PAg protected hamsters and cyclophosphamide-treated mice from lethal infection of serovar copenhageni and induced agglutinating antibodies against the four serovars in the same degrees as vaccines. These results suggested that the tetra-valent PAgs might be useful as a component vaccine against leptospiral infection instead of formalized whole cells vaccines for human.

Agglutination Tests↗
PubMed1996

Immunochemical characteristics and localization on cells of protective antigen (PAg) prepared from Leptospira interrogans serovar lai.

Immuno-electron microscopic methods revealed that the protective antigen (PAg) of Leptospira interrogans serovar lai exists on the outer envelope sheathing the leptospiral cell body. PAg lost its protective activity after treatment by hydrolysis with 2 M formic acid at 100 C for 2 hr, or oxidation with periodate at 4 C for 40 hr. The antigenic oligosaccharide fraction was further purified from the hydrolyzed PAg by immunoaffinity column coupled with protective monoclonal antibody, LW2, and by gel filtration of HPLC. The antigenic oligosaccharide fraction contained two unknown sugars and 4-O-methylmannose (molar ratio 3:5:1). These findings suggested that these sugars are components of an antigenic determinant contributing to the protective immunity against serovar lai infection.

Antigens, Bacterial↗
PubMed2003

Probable laboratory contamination of clinical specimens with Leptospira meyeri.

Leptospira meyeri were isolated from the blood or the pleural effusion cultures of four patients at a commercial clinical laboratory. All isolates were identical in their 16S rDNA sequences and NotI or SfiI restriction profiles of the chromosome DNA on pulsed-field gel electrophoresis. However, intraperitoneal inoculation of the isolate (NIID1) failed to kill hamsters and none of the patients' sera reacted with L. meyeri strains isolated, indicating leptospiral contamination occurred during laboratory investigation.

Animals↗
PubMed2005

Serological evidence of the persistence of infection with Leptospira interrogans serovar Hardjo in cattle in Mongolia.

Serum samples were collected randomly from Mongol breed cattle in three geographically distinct provinces of Mongolia. Antibodies specific to Leptospira interrogans serovar Hardjo were detected by microscopic agglutination test (MAT) at titres of 100 or more in 80.4% (86/107) of the samples from Dornod Province, but in only 28.9% (13/45) in Arkhangai and 23.5% (12/51) in Khuvsgul Provinces, respectively. Treatment of 9 serum samples from Dornod, positive to serovar Hardjo in MAT and negative in the homologous immunoglobulin G (IgG) enzyme-linked immunosorbent assay (ELISA), with 2-mercaptoethanol (2-ME) indicated that those animals were recently infected.

Agglutination Tests↗
PubMed1994

Prevalence of antibodies to different Leptospira interrogans serovars in pigs on large farms.

A seroepidemiological survey was carried out in the province of Badajoz (south-western Spain) in order to determine the presence and spread of Leptospira interrogans. The 521 sera tested were drawn from breeding sows on 28 large farms (15 with fewer than 60 and 13 with over 60 breeders). Immunological testing was performed using the Martin-Pettit micro-agglutination technique. Pigs with titres equal to or greater than 1:100 were considered positive. Haemolysed and/or contaminated test sera were reprocessed following filter-paper treatment. A total of 10.56% of pigs tested proved positive, 39.28% of farms being affected. The following L. interrogans serovars were detected: pomona (6.53%), castellonis (1.15%), sejroe (1.15%), grippotyphosa (0.96%), australis (0.38%), hebdomadis (0.19%) and icterohaemorrhagiae (0.19%).

Animals↗
PubMed1994

Immunochemical studies of opsonic epitopes of the lipopolysaccharide of Leptospira interrogans serovar hardjo.

Leptospiral lipopolysaccharides (LPS) are the main antigens responsible for immunity in leptospirosis. In this investigation we studied the nature of the antigenic determinants of LPS extracted from Leptospira interrogans serovar hardjo (reference strain Hardjoprajitno). The reactions of anti-LPS monoclonal antibodies (mAbs) MUM/F1-4/hardjo (IgM) and MUM/F1-6/hardjo (IgG) with whole cell lysates in Western immunoblotting analysis were unaffected by proteinase K treatment. Periodate treatment of the LPS destroyed the binding of MUM/F1-6/hardjo but preserved that of MUM/F1-4/hardjo. Alkaline phosphatase decreased significantly the binding of MUM/F1-4/hardjo to the LPS but only slightly that of MUM/F1-6/hardjo. On the other hand, phosphodiesterase totally destroyed the binding capacity of both monoclonal antibodies in enzyme immunoassays (EIA). A number of mono- and oligosaccharides was used in EIA inhibition studies. Mannose-6-phosphate and galactose-6-phosphate inhibited the binding of MUM/F1-4/hardjo (50% inhibition at a concentration of 5 mM) to the antigen, but glucose-6-phosphate did not. Galactosamine and mannosamine inhibited the binding of MUM/F1-6/hardjo (50% inhibition at a concentration of 3-4 mM), whereas only a weak inhibition was observed with glucosamine. In contrast, N-acetylated amino sugars did not show any inhibition. An O-acetyl group also appears to be involved in the antigen-antibody binding process.

Antibodies, Bacterial↗
PubMed1989

Monoclonal antibodies reacting with serogroup and serovar specific epitopes on different lipopolysaccharide subunits of Leptospira interrogans serovar pomona.

Monoclonal antibodies with two kinds of specificities, produced against Leptospira interrogans serovar pomona, were studied by agglutination and immunoblotting. Antibodies reacted either exclusively with serovar pomona or with all members of the Pomona serogroup, but none of the antibodies reacted with representative serovars of other serogroups. Both antibodies recognized epitopes on purified lipopolysaccharide (LPS) from serovar pomona. In immunoblotting experiments the serogroup specific antibody recognized both the major LPS bands of 21 kDa and 26 kDa whereas the serovar specific antibodies reacted only with the 26 kDa band, thus localizing serovar specificity in the 26 kDa band and serogroup specific epitopes on at least two different LPS subunits.

Animals↗
PubMed1992

Immunodominant antigens recognized by the human immune response to infection by organisms of the species Leptospira interrogans serogroup Australis.

Serum samples from patients infected by organisms of Leptospira interrogans serogroup Australis were tested by Western blot to determine the nature of major antigens that are involved in the immune response. Although there was some patient-to-patient variability, immunodominant genus-specific antigens were found to be proteins of apparent molecular ratio 68, 46 and 35-kDa, and lipopolysaccharide (LPS) sub-units in the 35-14-kDa region. Serogroup epitopes specific for Australis were exclusively saccharides of about 32 and 24 kDa: a serovar-specific antigen for serovar lora was of 38-40 kDa and behaved like a protein. Antibodies to the LPS serogroup-specific antigens and to the 38-40 kDa protein were long-lasting and consequently suggest that these immunodominant epitopes are important in resistance to re-infection.

Antibodies, Bacterial↗
PubMed1997

Oligonucleotides specific for pathogenic and saprophytic leptospira occurring in water.

Sets of primers specific for both pathogenic (SPL) and saprophytic (SSL) Leptospira were designed from ribosomal 16S genes (rrs) available in databases. They were used as two sets of primer pairs for the PCR amplification of known pathogenic and saprophytic strains. It was possible to identify pathogenic strains by the use of SPL primers and saprophytic ones by SSL primers. Serovars from L. meyeri, of controversial pathogenicity status, confirmed the heterogeneity of the species representatives in this respect. Serovars ranarum, sofia and perameles were amplified by SPL and not SSL. Conversely, serovar semaranga was amplified by SSL and not SPL. In order to use SPL primers for the detection of pathogenic leptospires from a natural water environment, we set up an additional semi-nested PCR by employing a second internal primer which succeeded in detecting as few as 5 pathogenic leptospires per ml of water.

DNA, Bacterial↗
PubMed2000

Characterization of the Leptospira interrogans S10-spc-alpha operon.

A ribosomal protein gene cluster from the spirochaete Leptospira interrogans was characterized. This locus is homologous to the Escherichia coli S10, spc, and alpha operons. Analysis of L. interrogans RNA showed that the ribosomal protein genes within this cluster are co-transcribed, thus forming an operon. Two transcription initiation sites were mapped by primer extension, upstream of fus, the first gene in this cluster, and sequences from this region provided promoter activity in E. coli. Transcription terminates near a predicted stem-loop structure following rplQ, the last gene in the cluster. These data suggest that two promoters upstream of fus direct transcription of this 17.5-kb ribosomal protein gene cluster. Comparison of the L. interrogans S10-spc-alpha cluster to homologous loci from Borrelia burgdorferi and Treponema pallidum provided evidence that this region of the genome underwent several rearrangements during spirochaete evolution.

Bacterial Proteins↗
PubMed2000

Identification of a 36-kDa fibronectin-binding protein expressed by a virulent variant of Leptospira interrogans serovar icterohaemorrhagiae.

We investigated the ability of a virulent strain of Leptospira interrogans serovar icterohaemorrhagiae, its isogenic avirulent variant and a saprophytic strain to bind fibronectin using alkaline phosphatase-labelled fibronectin. A single 36-kDa fibronectin-binding protein was expressed only by the virulent strain and was located in the outer sheath according to proteinase K treatment results. The interaction of this protein with fibronectin was specific and the region of fibronectin bound to this potential adhesin overlapped the gelatin-binding domain. The inability of a RGDS synthetic peptide to inhibit the binding of fibronectin indicated that the cell-binding domain was not involved in this interaction. Considering the wide distribution of fibronectin within a host and the diversity of mammals involved in the epidemiology of leptospirosis, its implication in the cell attachment process of virulent leptospires is coherent with the multiplicity of target cells.

Adhesins, Bacterial↗
PubMed2005

Identification and classification of all potential hemolysin encoding genes and their products from Leptospira interrogans serogroup Icterohae-morrhagiae serovar Lai.

AIM: To identify and classify all potential hemolysin candidates of Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai. METHODS: All of the potential hemolysin encoding genes were characterized in silico. These genes were cloned and expressed in Escherichia coli. The hemolytic activities of the expressed proteins were assayed observing the hemolysis on sheep blood agar plates. Sphingomyelinase activities of the hemolysin candidates were measured by thin-layer chromatography (TLC) and HPLC for sphingomyelin-hydrolysis. Expression and secretion of the hemolysins in L interrogans were studied by reverse transcription polymerase chain reaction, Western blot, and enzyme-linked immunosorbent assays. RESULTS AND CONCLUSION: The hemolytic activities of hemolysin candidates (LA0327, LA0378, LA1027, LA1029, LA1650, LA3050, LA3937, LA4004) from L interrogans strain Lai were confirmed. They were further divided into two groups, sphingomyelinase hemolysins and non-sphingomyelinase hemolysins, based on their ability to hydrolyze sphingomyelin. Most of these hemolysins were actually expressed in living L interrogans and some of them were secreted into the environment. This study establishes an essential and complete basis for further studying the contribution of hemolysins to the pathogenesis of L interrogans.

Amino Acid Sequence↗
PubMed2006

Characterization of cheW genes of Leptospira interrogans and their effects in Escherichia coli.

The motility and chemotaxis systems are critical for the virulence of leptospires. In this study, the phylogenetic profiles method was used to predict the interaction of chemotaxis proteins. It was shown that CheW1 links to CheA1, CheY, CheB and CheW2; CheW3 links to CheA2, MCP (LA2426), CheB3 and CheD1; and CheW2 links only to CheW1. The similarity analysis demonstrated that CheW2 of Leptospira interrogans strain Lai had poor homology with CheW of Escherichia coli in the region of residues 30-50. In order to verify the function of these proteins, the putative cheW genes were cloned into pQE31 vector and expressed in wild-type E. coli strain RP437 or cheW defective strain RP4606. The swarming results indicated that CheW1 and CheW3 could restore swarming of RP4606 while CheW2 could not. Overexpression of CheW1 and CheW3 in RP437 inhibited the swarming of RP437, whereas the inhibitory effect of CheW2 was much lower. Therefore, we presumed that CheW1 and CheW3 might have the function of CheW while CheW2 does not. The existence of multiple copies of chemotaxis homologue genes suggested that L. interrogans strain Lai might have a more complex chemosensory pathway.

Amino Acid Sequence↗
PubMed1980

Leptospira interrogans serovar hardjo vaccination of pregnant beef cows and subsequent growth rate of progeny.

Five experiments with Leptospira interrogans serovar hardjo vaccine were carried out over a 6-year period in pregnant Brahman-cross and Sahiwal-cross cows in the dry tropics on northern Queensland. The numbers ranged from 127 breeders aged 2 to 5 years in 1972 to 344 breeders aged 2 to 9 years in 1977. Half of the cows were vaccinated twice in mid-pregnancy except for 1977, when they were vaccinated once. In 1975-1977 inclusive, half of the heifers were given an additional dose of vaccine at commencement of mating. Vaccination caused a significant (P less than 0.01) reduction of prenatal loss but not of perinatal or postnatal losses. Growth rates of calves from vaccinated and unvaccinated dams were similar.

Animals↗
PubMed1980

Leptospira serogroup Hebdomadis infection as an Australian zoonosis.

Two cases of leptospirosis due to infection with a member of the Hebdomadis serogroup are described in farm workers on a Victorian dairy farm. The source of infection appeared to be the milking herd which had elevated serum antibody titres against a member of the Hebdomadis serogroup. Agglutinin-absorption testing of one patient's serum indicated that the infecting serovar was hardjo. A survey of 1,144 cattle entering abattoirs throughout the State indicated that 44.3% of these animals showed serological evidence of past or present infection with leptospira of the Hebdomadis serogroup and the potential risk for people with occupational contact with cattle is emphasised. The importance of considering leptospirosis in the differential diagnosis of all patients with influenza-like symptoms or pyrexia of unknown origin and having occupational contact with animals, especially cattle, is discussed.

Animals↗
PubMed1980

The prevalence of antibodies to members of Leptospira interrogans in cattle.

A total of 1,355 random samples taken from bovine serums submitted for brucellosis testing in Victoria were submitted to the microscopic agglutination test for the presence of antibody to 12 serovars of Leptospira interrogans. The most common reaction obtained was to serovar hardjo, although the percentage of reactors varied from 24.8% in the metropolitan area to 56.3% in north-eastern Victoria (mean 40.6%). A total of 86.3% of farms from which 3 or more samples were taken had at least one reactor to serovar hardjo. The prevalence of antibody to other serovars was tarassovi (7.8% of reactors), ballum (3.7%), pomona (2.4%), autumnalis (1.8%) and bataviae (1.2%). Reactions to other serovars were observed in serums of less than 1% of cattle tested; serums from 50.8% of cattle did not react to any antigen.

Agglutination Tests↗