Leptospirosis during Dengue Outbreak, Bangladesh

LaRocque, Regina C.; Breiman, Robert F; Ari, Mary D.; Morey, Roger E.; Janan, Firdous Ara; Hayes, John Mosely; Hossain, M. Anowar; Brooks, W. Abdullah; Levett, Paul N.

doi:10.3201/eid1105.041212

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Leptospirosis during Dengue Outbreak, Bangladesh

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Author(s): Regina C. LaRocque ^* ^, , Robert F. Breiman ^† , Mary D. Ari ^‡ , Roger E. Morey ^‡ , Firdous Ara Janan ^§ , John Mosely Hayes ^¶ , M. Anowar Hossain ^† , W. Abdullah Brooks ^† , Paul N. Levett ^‡

Publication date (Print): May 2005

Journal: Emerging Infectious Diseases

Publisher: Centers for Disease Control and Prevention

Keywords: Leptospirosis, Dengue, Bangladesh, fever

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Abstract

We collected acute-phase serum samples from febrile patients at 2 major hospitals in Dhaka, Bangladesh, during an outbreak of dengue fever in 2001. A total of 18% of dengue-negative patients tested positive for leptospirosis. The case-fatality rate among leptospirosis patients (5%) was higher than among dengue fever patients (1.2%).

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Most cited references 13

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The leptospiral major outer membrane protein LipL32 is a lipoprotein expressed during mammalian infection.

D Haake, J Matsunaga, C Bolin … (2000)

We report the cloning of the gene encoding the 32-kDa lipoprotein, designated LipL32, the most prominent protein in the leptospiral protein profile. We obtained the N-terminal amino acid sequence of a staphylococcal V8 proteolytic-digest fragment to design an oligonucleotide probe. A Lambda-Zap II library containing EcoRI fragments of Leptospira kirschneri DNA was screened, and a 5.0-kb DNA fragment which contained the entire structural lipL32 gene was identified. Several lines of evidence indicate that LipL32 is lipid modified in a manner similar to that of other procaryotic lipoproteins. The deduced amino acid sequence of LipL32 would encode a 272-amino-acid polypeptide with a 19-amino-acid signal peptide, followed by a lipoprotein signal peptidase cleavage site. LipL32 is intrinsically labeled during incubation of L. kirschneri in media containing [(3)H]palmitate. The linkage of palmitate and the amino-terminal cysteine of LipL32 is acid labile. LipL32 is completely solubilized by Triton X-114 extraction of L. kirschneri; phase separation results in partitioning of LipL32 exclusively into the hydrophobic, detergent phase, indicating that it is a component of the leptospiral outer membrane. CaCl(2) (20 mM) must be present during phase separation for recovery of LipL32. LipL32 is expressed not only during cultivation but also during mammalian infection. Immunohistochemistry demonstrated intense LipL32 reactivity with L. kirschneri infecting proximal tubules of hamster kidneys. LipL32 is also a prominent immunogen during human leptospirosis. The sequence and expression of LipL32 is highly conserved among pathogenic Leptospira species. These findings indicate that LipL32 may be important in the pathogenesis, diagnosis, and prevention of leptospirosis.

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Detection of pathogenic leptospires by real-time quantitative PCR.

Paul N. Levett, Roger Morey, Renee L. Galloway … (2005)

Definitive diagnosis of leptospirosis has traditionally depended upon the isolation of leptospires from clinical specimens or the demonstration of seroconversion in paired acute and convalescent serum samples. Both of these approaches require expertise not routinely available in clinical laboratories and usually result in delayed diagnosis. Conventional PCR assays have been developed, but all have limitations which have restricted their widespread use. In order to overcome these limitations, a real-time PCR assay was developed using a 423 bp target on the lipL32 gene, which is conserved among pathogenic serovars of LEPTOSPIRA: Reactions were monitored by SYBR green fluorescence and melting curve analysis. Representative serovars from 16 species of Leptospira and over 40 species of other bacteria and fungi were tested. Positive results were obtained with all pathogenic leptospiral serovars, with the exception of Leptospira fainei serovar Hurstbridge. The analytical sensitivity of this assay was 3 genome equivalents per reaction; approximately 10 genome equivalents were detectable in human urine. Leptospiral DNA was amplified from blood containing EDTA or citrate anticoagulants, but heparin, sodium polyanetholesulfonate and saponin were inhibitory. The assay successfully detected leptospiral DNA from serum and urine samples of patients with leptospirosis. This assay has the potential to facilitate rapid, sensitive diagnosis of acute leptospirosis.

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Evaluation of four commercially available rapid serologic tests for diagnosis of leptospirosis.

R. Spiegel, M D Bajani, S Bragg … (2003)

Four rapid tests for the serologic diagnosis of leptospirosis were evaluated, and the performance of each was compared with that of the current standard, the microscopic agglutination test (MAT). The four rapid tests were a microplate immunoglobulin M (IgM)-enzyme-linked immunosorbent assay (ELISA), an indirect hemagglutination assay (IHA), an IgM dipstick assay (LDS), and an IgM dot-ELISA dipstick test (DST). A panel of 276 sera from 133 cases of leptospirosis from four different geographic locations was tested as well as 642 sera from normal individuals or individuals with other infectious or autoimmune diseases. Acute-phase sera from cases (n = 148) were collected or=15 days after onset (median = 29.1). By a traditional method (two-by-two contingency table), the sensitivities for detection of leptospirosis cases were 93.2% by LDS, 92.5% by DST, 86.5% by ELISA, and 79.0% by IHA. Specificity was 98.8% by DST, 97% by ELISA and MAT, 95.8% by IHA, and 89.6% by LDS. With a latent class analysis (LCA) model that included all the rapid tests and the clinical case definition, sensitivity was 95.5% by DST, 94.5% by LDS, 89.9% by ELISA, and 81.1% by IHA. The sensitivity and specificity estimated by the traditional methods were quite close to the LCA estimates. However, LCA allowed estimation of the sensitivity of the MAT (98.2%), which traditional methods do not allow. For acute-phase sera, sensitivity was 52.7% by LDS, 50.0% by DST, 48.7% by MAT and ELISA, and 38.5% by IHA. The sensitivity for convalescent-phase sera was 93.8% by MAT, 84.4% by DST, 83.6% by LDS, 75.0% by ELISA, and 67.2% by IHA. A good overall correlation with the MAT was obtained for each of the assays, with the highest concordance being with the DST (kappa value, 0.85; 95% confidence interval [CI], 0.8 to 0.90). The best correlation was between ELISA and DST (kappa value, 0.86; 95% CI, 0.81 to 0.91). False-positive LDS results were frequent (>or=20%) in sera from individuals with Epstein-Barr virus, human immunodeficiency virus, and periodontal disease and from healthy volunteers. The ease of use and significantly high sensitivity and specificity of DST and ELISA make these good choices for diagnostic testing.

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Author and article information

Journal

Journal ID (nlm-ta): Emerg Infect Dis

Journal ID (iso-abbrev): Emerging Infect. Dis

Journal ID (publisher-id): EID

Title: Emerging Infectious Diseases

Publisher: Centers for Disease Control and Prevention

ISSN (Print): 1080-6040

ISSN (Electronic): 1080-6059

Publication date (Print): May 2005

Volume: 11

Issue: 5

Pages: 766-769

Affiliations

[* ]Massachusetts General Hospital, Boston, Massachusetts, USA;

[† ]International Centre for Diarrhoeal Disease Research, Bangladesh, Dhaka, Bangladesh;

[‡ ]Centers for Disease Control and Prevention, Atlanta, Georgia, USA;

[§ ]Dhaka Medical College Hospital, Dhaka, Bangladesh;

[¶ ]Centers for Disease Control and Prevention, San Juan, Puerto Rico, USA

Author notes

Address for correspondence: Regina C. LaRocque, Division of Infectious Diseases, Gray-Jackson 504, Massachusetts General Hospital, 55 Fruit St, Boston, MA 02114, USA; fax: 617-726-7416; email: rclarocque@ 123456partners.org

Article

Publisher ID: 04-1212

DOI: 10.3201/eid1105.041212

PMC ID: 3320387

PubMed ID: 15890136

SO-VID: f4713632-57f9-4d97-9d44-0b060bb6417f

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Leptospirosis during Dengue Outbreak, Bangladesh

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Zika Virus

Most cited references 13

The leptospiral major outer membrane protein LipL32 is a lipoprotein expressed during mammalian infection.

Detection of pathogenic leptospires by real-time quantitative PCR.

Evaluation of four commercially available rapid serologic tests for diagnosis of leptospirosis.

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