Author | Murray, Gerald L | |
Author | Srikram, Amporn | |
Author | Hoke, David E | |
Author | Wunder Junior, Elsio Augusto | |
Author | Henry, Rebekah | |
Author | Lo, Miranda | |
Author | Zhang, Kunkun | |
Author | Sermswan, Rasana W | |
Author | Ko, Albert Icksang | |
Author | Adler, Ben | |
Access date | 2015-11-20T14:24:16Z | |
Available date | 2015-11-20T14:24:16Z | |
Document date | 2009 | |
Citation | MURRAY, G. L. et al. Major surface protein LipL32 is not required for either acute or chronic infection with Leptospira interrogans. Infection and Immunity, v. 77, n. 3, p. 952-958, 2009. | pt_BR |
ISSN | 1098-5522 | |
URI | https://www.arca.fiocruz.br/handle/icict/12298 | |
Language | eng | pt_BR |
Publisher | American Society of Microbiology | pt_BR |
Rights | open access | pt_BR |
Title | Major surface protein LipL32 is not required for either acute or chronic infection with Leptospira interrogans. | pt_BR |
Type | Article | pt_BR |
DOI | 10.1128/IAI.01370-08 | |
Abstract | Leptospira interrogans is responsible for leptospirosis, a zoonosis of worldwide distribution. LipL32 is the
major outer membrane protein of pathogenic leptospires, accounting for up to 75% of total outer membrane
protein. In recent times LipL32 has become the focus of intense study because of its surface location,
dominance in the host immune response, and conservation among pathogenic species. In this study, an lipL32
mutant was constructed in L. interrogans using transposon mutagenesis. The lipL32 mutant had normal
morphology and growth rate compared to the wild type and was equally adherent to extracellular matrix.
Protein composition of the cell membranes was found to be largely unaffected by the loss of LipL32, with no
obvious compensatory increase in other proteins. Microarray studies found no obvious stress response or
upregulation of genes that may compensate for the loss of LipL32 but did suggest an association between
LipL32 and the synthesis of heme and vitamin B12. When hamsters were inoculated by systemic and mucosal
routes, the mutant caused acute severe disease manifestations that were indistinguishable from wild-type L.
interrogans infection. In the rat model of chronic infection, the LipL32 mutant colonized the renal tubules as
efficiently as the wild-type strain. In conclusion, this study showed that LipL32 does not play a role in either
the acute or chronic models of infection. Considering the abundance and conservation of LipL32 among all
pathogenic Leptospira spp. and its absence in saprophytic Leptospira, this finding is remarkable. The role of this
protein in leptospiral biology and pathogenesis thus remains elusive. | pt_BR |
Affilliation | Monash University. Australian Bacterial Pathogenesis Program / Australian Research Council Centre of Excellence in Structural. Clayton, Australia | pt_BR |
Affilliation | Khon Kaen University. Faculty of Medicine. Melioidosis Research Center. Department of Biochemistry. Khon Kaen, Thailand | pt_BR |
Affilliation | Monash University. Australian Bacterial Pathogenesis Program / Australian Research Council Centre of Excellence in Structural. Clayton, Australia | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil | pt_BR |
Affilliation | Monash University. Australian Bacterial Pathogenesis Program / Australian Research Council Centre of Excellence in Structural. Clayton, Australia | pt_BR |
Affilliation | Monash University. Australian Bacterial Pathogenesis Program / Australian Research Council Centre of Excellence in Structural. Clayton, Australia | pt_BR |
Affilliation | Monash University. Functional Microbial Genomics. Department of Microbiology. Clayton, Australia | pt_BR |
Affilliation | Khon Kaen University. Faculty of Medicine. Khon Kaen, Thailand | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil / Weill Medical College of Cornell University. Division of International Medicine and Infectious Disease. New York, New York | pt_BR |
Affilliation | Monash University. Australian Bacterial Pathogenesis Program / Australian Research Council Centre of Excellence in Structural. Clayton, Australia / Monash University. Functional Microbial Genomics. Department of Microbiology. Clayton, Australia | pt_BR |
DeCS | Proteínas da Membrana Bacteriana Externa/metabolismo | pt_BR |
DeCS | Leptospira interrogans/patogenicidade | pt_BR |
DeCS | Leptospirose/metabolismo | pt_BR |
DeCS | Lipoproteínas/metabolismo | pt_BR |
DeCS | Animais | pt_BR |
DeCS | Proteínas da Membrana Bacteriana Externa/genética | pt_BR |
DeCS | Western Blotting | pt_BR |
DeCS | Cricetinae | pt_BR |
DeCS | Leptospira interrogans/genética | pt_BR |
DeCS | Leptospira interrogans/metabolismo | pt_BR |
DeCS | Leptospirose/genética | pt_BR |
DeCS | Mesocricetus | pt_BR |
DeCS | Análise de Sequência com Séries de Oligonucleotídeos | pt_BR |
DeCS | Reação em Cadeia da Polimerase | pt_BR |
DeCS | Ratos | pt_BR |
DeCS | Ratos Wistar | pt_BR |