The Leptospira interrogans LIC10774 is a multifunctional surface protein that binds calcium and interacts with host components

Passalia, Felipe José; Carvalho, Enéas; Heinemann, Marcos Bryan; Vieira, Mônica L.; Nascimento, Ana L. T. O.

doi:10.1016/j.micres.2020.126470

Cited by 5 publications

(13 citation statements)

References 81 publications

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“…The recombinant protein LIC13086 interacts with ECM laminin with high affinity based on K D value, comparable with the putative adhesins Lsa23, Lsa46, and rLIC10774, previously reported ( Domingos et al., 2012 ; Teixeira et al., 2015 ; Passalia et al., 2020a ). It also interacts with other host plasma factors and exhibits a redundant multiple-binding profile like other characterized outer membrane proteins ( Vieira et al., 2014 ).…”

Section: Discussionsupporting

confidence: 85%

“…Moreover, the rLIC13086 acquisition of fibrinogen and plasma fibronectin from NHS may reflect what happens in vivo and the mechanism by which LIC13086 participates in the reduction of fibrin clot formation. The features describe for rLIC13086 contrast with the previously described leptospiral protein rLIC10774 ( Passalia et al., 2020a ). The latter is a Ca 2+ -binding protein and although interacting with fibrinogen, does not inhibit fibrin clot formation.…”

Section: Discussionmentioning

confidence: 89%

“…A well-known mechanism used by leptospires to reach different infection targets and survive during dissemination is the acquisition of host proteases to degrade ECM components and complement proteins. It has been described that pathogenic leptospires can capture circulating plasminogen via multiple surface-exposed proteins, which are then converted into plasmin by host activators ( Vieira et al., 2010a ; Vieira et al., 2012 ; Kochi et al., 2019 ; Passalia et al., 2020a ). The Leptospira -associated plasmin acts by degrading several host molecules during the infection process ( Vieira et al., 2013 ; Vieira and Nascimento, 2016 ; Vieira et al., 2020b ).…”

Section: Discussionmentioning

confidence: 99%

“…The initial process of infection consists of leptospires’ adhesion onto extracellular matrix molecules in the host epithelial skin tissue. This step is mediated by leptospiral outer membrane adhesins, of which several were already characterized ( Vieira et al., 2014 ; Figueredo et al., 2017 ; Pereira et al., 2017 ; Cavenague et al., 2019 ; Kochi et al., 2019 ; Rossini et al., 2019 ; Passalia et al., 2020a ). When leptospires reach the bloodstream, they are able to interact with circulating host plasma components ( Vieira et al., 2020 ).…”

Section: Introductionmentioning

confidence: 99%

“…Surface exposed protein in leptospires can interact with human fibrinogen leading to a partial inhibition of fibrin clot formation thus facilitating the dissemination ( Oliveira et al., 2013 ; Fernandes et al., 2015 ). Furthermore, several leptospiral surface proteins interact with regulators and components of the host complement system as a mechanism of innate immune evasion ( Siqueira et al., 2017 ; Cavenague et al., 2019 ; Kochi et al., 2019 ; Passalia et al., 2020a ).…”

Section: Introductionmentioning

confidence: 99%

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A Novel Leptospira interrogans Protein LIC13086 Inhibits Fibrin Clot Formation and Interacts With Host Components

Passalia

Heinemann

Vieira

et al. 2021

Front. Cell. Infect. Microbiol.

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Leptospirosis is a neglected zoonosis, caused by pathogenic spirochetes bacteria of the genus Leptospira. The molecular mechanisms of leptospirosis infection are complex, and it is becoming clear that leptospires express several functionally redundant proteins to invade, disseminate, and escape the host’s immune response. Here, we describe a novel leptospiral protein encoded by the gene LIC13086 as an outer membrane protein. The recombinant protein LIC13086 can interact with the extracellular matrix component laminin and bind plasminogen, thus possibly participating during the adhesion process and dissemination. Also, by interacting with fibrinogen and plasma fibronectin, the protein LIC13086 probably has an inhibitory effect in the fibrin clot formation during the infection process. The newly characterized protein can also bind molecules of the complement system and the regulator C4BP and, thus, might have a role in the evasion mechanism of Leptospira. Taken together, our results suggest that the protein LIC13086 may have a multifunctional role in leptospiral pathogenesis, participating in host invasion, dissemination, and immune evasion processes.

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Section: Discussionsupporting

confidence: 85%

Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

A Novel Leptospira interrogans Protein LIC13086 Inhibits Fibrin Clot Formation and Interacts With Host Components

Passalia

Heinemann

Vieira

et al. 2021

Front. Cell. Infect. Microbiol.

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Protective efficacy evaluation of immunogenic protein AHA_3793 of Aeromonas hydrophila as vaccine candidate for largemouth bass Micropterus salmoides

et al. 2022

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A bstractAeromonas hydrophila is a Gram-negative pathogen that can infect various fi sh, including largemouth bass ( Micropterus salmoides ), which have caused huge economic losses. In present study, largemouth bass anti-A . hydrophila antibodies were produced, then a highly immunogenic outer membrane proteins, AHA_3793, was identifi ed by combined western blotting and mass spectrometry analysis. Moreover, AHA_3793 was expressed, and its immunogenicity was further verifi ed by western blotting. Subsequently, the protective effi cacy of AHA_3793 were evaluated in largemouth bass. The results showed that rAHA_3793 could produce a relative percentage survival (RPS) of 61.76% for largemouth bass against A . hydrophila challenge. ELISA analysis showed the specifi c serum antibodies of largemouth bass against rAHA_3793 and A . hydrophila in vaccinated group in weeks 4 and 5 after immunization were signifi cantly higher than those in control group, which suggested that rAHA_3793 induced production of specifi c serum antibodies against rAHA_3793 and A . hydrophila . The qRT-PCR analysis showed that expressions of CD4-2 and MHC IIα were also signifi cantly up-regulated after immunization. These results collectively demonstrated that rAHA_3793 could induce a strong humoral immune response of largemouth bass, and then produce high immune protection eff ects against A . hydrophila infection.

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The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components

Takahashi

Nascimento

2021

Virulence

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The Leptospira interrogans LIC10774 is a multifunctional surface protein that binds calcium and interacts with host components

Cited by 5 publications

References 81 publications

A Novel Leptospira interrogans Protein LIC13086 Inhibits Fibrin Clot Formation and Interacts With Host Components

A Novel Leptospira interrogans Protein LIC13086 Inhibits Fibrin Clot Formation and Interacts With Host Components

Protective efficacy evaluation of immunogenic protein AHA_3793 of Aeromonas hydrophila as vaccine candidate for largemouth bass Micropterus salmoides

The leptospiral LipL21 and LipL41 proteins exhibit a broad spectrum of interactions with host cell components

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