Leptospiral extracellular matrix adhesins as mediators of pathogen-host interactions

Vieira, Mônica L.; Fernandes, Luis G. V.; Domingos, Renan F.; Oliveira, Rômulo Silva de; Siqueira, Gabriela H.; Souza, Natalie M.; Teixeira, Aline F.; Atzingen, Marina V.; Nascimento, Ana L. T. O.

doi:10.1111/1574-6968.12349

Cited by 61 publications

(51 citation statements)

References 66 publications

(86 reference statements)

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“…Lsa27, which are laminin-binding adhesins (Barbosa et al, 2006), and distinct from those of other adhesins, which have been reported to have broader characteristics of binding to ECM macromolecules (Stevenson et al, 2007;Vieira et al, 2014). These results were expected since we have previously reported that Leptospira adhere to several ECM macromolecules, including laminin, collagen I, collagen IV, cellular fibronectin and plasma fibronectin (Barbosa et al, 2006).…”

Section: Ipmentioning

confidence: 70%

Novel Leptospira interrogans protein Lsa32 is expressed during infection and binds laminin and plasminogen

Domingos¹,

Fernandes²,

Romero³

et al. 2015

Microbiology

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Pathogenic Leptospira is the aetiological agent of leptospirosis, a life-threatening disease of human and veterinary concern. The quest for novel antigens that could mediate host-pathogen interactions is being pursued. Owing to their location, these antigens have the potential to elicit numerous activities, including immune response and adhesion. This study focuses on a hypothetical protein of Leptospira, encoded by the gene LIC11089, and its three derived fragments: the N-terminal, intermediate and C terminus regions. The gene coding for the full-length protein and fragments was cloned and expressed in Escherichia coli BL21(SI) strain by using the expression vector pAE. The recombinant protein and fragments tagged with hexahistidine at the N terminus were purified by metal affinity chromatography. The leptospiral full-length protein, named Lsa32 (leptospiral surface adhesin, 32 kDa), adheres to laminin, with the C terminus region being responsible for this interaction. Lsa32 binds to plasminogen in a dose-dependent fashion, generating plasmin when an activator is provided. Moreover, antibodies present in leptospirosis serum samples were able to recognize Lsa32. Lsa32 is most likely a new surface protein of Leptospira, as revealed by proteinase K susceptibility. Altogether, our data suggest that this multifaceted protein is expressed during infection and may play a role in host-L. interrogans interactions.

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Section: Ipmentioning

confidence: 70%

Novel Leptospira interrogans protein Lsa32 is expressed during infection and binds laminin and plasminogen

Domingos¹,

Fernandes²,

Romero³

et al. 2015

Microbiology

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“…Recently, a varied collection of ECM-binding proteins has been identified, suggesting cross-reaction of adhesion molecules that probably form part of invasion mechanisms of Leptospira (Fouts et al, 2016). Multi-functional putative adhesins that bind to the plasminogen were also characterized Vieira et al, 2014;Domingos et al, 2015), although the role of environmental biotic or abiotic structures in the biology of saprophytes is still unclear (Fouts et al, 2016). Previous studies have documented Leptospira, PLA reducing C3b and human IgG deposition, thereby impairing opsonization and restricting complement antibacterial functions .…”

Section: Advances On Proteomics Of Leptospiramentioning

confidence: 99%

Pathogenic <i>Leptospira</i>: Advances in understanding the molecular pathogenesis and virulence

Ghazaei¹

2018

Open Vet J.

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Leptospirosis is a common zoonotic disease has emerged as a major public health problem, with developing countries bearing disproportionate burdens. Although the diverse range of clinical manifestations of the leptospirosis in humans is widely documented, the mechanisms through which the pathogen causes disease remain undetermined. In addition, leptospirosis is a much-neglected life-threatening disease although it is one of the most important zoonoses occurring in a diverse range of epidemiological distribution. Recent advances in molecular profiling of pathogenic species of the genus Leptospira have improved our understanding of the evolutionary factors that determine virulence and mechanisms that the bacteria employ to survive. However, a major impediment to the formulation of intervention strategies has been the limited understanding of the disease determinants. Consequently, the association of the biological mechanisms to the pathogenesis of Leptospira, as well as the functions of numerous essential virulence factors still remain implicit. This review examines recent advances in genetic screening technologies, the underlying microbiological processes, the virulence factors and associated molecular mechanisms driving pathogenesis of Leptospira species.

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“…11 Lig proteins are promiscuous adhesins and bind to a wide variety of extracellular proteins. 12 The Lig protein family is composed of the outer surface proteins LigA, LigB (Figure 1A), and LigC, which contain 13, 12, and 13 immunoglobulin-like (Ig-like) domains, respectively. 13−15 The N-terminal 630 amino acids of LigA and LigB (LigCon), covering the first 6 1 / 2 Ig-like domains, are highly conserved between the two Lig proteins, but the remaining C-terminal domains are variable (Figure 1A).…”

mentioning

confidence: 99%

NMR Solution Structure of the Terminal Immunoglobulin-like Domain from the Leptospira Host-Interacting Outer Membrane Protein, LigB

Ptak¹,

Hsieh²,

Lin³

et al. 2014

Biochemistry

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A number of surface proteins specific to pathogenic strains of Leptospira have been identified. The Lig protein family has shown promise as a marker in typing leptospiral isolates for pathogenesis and as an antigen in vaccines. We used NMR spectroscopy to solve the solution structure of the twelfth immunoglobulin-like (Ig-like) repeat domain from LigB (LigB-12). The fold is similar to that of other bacterial Ig-like domains and comprised mainly of β-strands that form a β-sandwich based on a Greek-key folding arrangement. Based on sequence analysis and conservation of structurally important residues, homology models for the other LigB Ig-like domains were generated. The set of LigB models illustrates the electrostatic differences between the domains as well as the possible interactions between neighboring domains. Understanding the structure of the extracellular portion of LigB and related proteins is important for developing diagnostic methods and new therapeutics directed toward leptospirosis.

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Leptospiral extracellular matrix adhesins as mediators of pathogen-host interactions

Cited by 61 publications

References 66 publications

Novel Leptospira interrogans protein Lsa32 is expressed during infection and binds laminin and plasminogen

Novel Leptospira interrogans protein Lsa32 is expressed during infection and binds laminin and plasminogen

Pathogenic <i>Leptospira</i>: Advances in understanding the molecular pathogenesis and virulence

NMR Solution Structure of the Terminal Immunoglobulin-like Domain from the Leptospira Host-Interacting Outer Membrane Protein, LigB

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