Correction to: Binding of Brucella protein, Bp26, to select extracellular matrix molecules

ElTahir, Yasmin; Al-Araimi, Amna; Nair, R.; Autio, Kaija J.; Tu, Hongmin; Leo, Jack C.; Al-Marzooqi, W.; Johnson, Eugene H.

doi:10.1186/s12860-020-00263-4

Cited by 3 publications

(2 citation statements)

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“…Brucella display on their surface several adhesion factors, necessary to adhere to and invade different cell types and tissues. Among these, the Brucella protein Bp26 is able to bind several ECM ligands, including Vn [91]. The protein binds Vn through different N-terminal domains (amino acids 46-65, 96-115 and 146-160) and through two regions located at the C-terminal domain (amino acids 176-190 and 231-250), suggesting the importance of this interaction for the bacterium (Table 1).…”

Section: Vitronectin-binding By Bacteria With a Yet To Be Defined Act...mentioning

confidence: 99%

Recruitment of Vitronectin by Bacterial Pathogens: A Comprehensive Overview

Pellegrini,

Pietrocola

2024

Preprint

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The key factor that enables pathogenic bacteria to establish successful infections lies largely in their ability to escape the host's immune response and adhere to host surfaces. Vitronectin (Vn) is a multi-domain glycoprotein ubiquitously present in blood and extracellular matrix of several tissues, where it plays important roles as regulator of membrane attack complex (MAC) formation and as mediator of cell adhesion. Vn has emerged as intriguing target for several microorganisms. Vn-binding by bacterial receptors confers protection from lysis resulting from MAC deposition. Furthermore, through its Arg-Gly-Asp (RGD) motif, Vn can bind several host cell integrins. Therefore, Vn recruited to the bacterial cell functions as a molecular bridge between bacteria and host surfaces, where it triggers several host signalling events that could promote bacterial internalisation. Each bacterium uses different receptors that recognise specific Vn-domains. In this review, we update the current knowledge of Vn receptors of major bacterial pathogens, emphasising the role they may play in the host upon Vn-binding. Focusing on the structural properties of bacterial proteins, we provide details on the residues involved in their interaction with Vn. Furthermore, we discuss the possible involvement of Vn adsorption on biomaterials in promoting bacterial adhesion on abiotic surfaces.

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Section: Vitronectin-binding By Bacteria With a Yet To Be Defined Act...mentioning

confidence: 99%

Recruitment of Vitronectin by Bacterial Pathogens: A Comprehensive Overview

Pellegrini,

Pietrocola

2024

Preprint

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“…More recently, in Brucella , a collagen-binding adhesin (major outer membrane protein, Bp26) was described by enzyme-linked immunosorbent assay (ELISA) and bio-layer interferometry. The protein was shown to bind to type I collagen, vitronectin, and soluble fibronectin ( ElTahir et al, 2019 ).…”

Section: Introductionmentioning

confidence: 99%

Non-adaptive Evolution of Trimeric Autotransporters in Brucellaceae

et al. 2020

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Brucella species are Gram-negative, facultative intracellular pathogens. They are the main cause of brucellosis, which has led to a global health burden. Adherence of the pathogen to the host cells is the first step in the infection process. The bacteria can adhere to various biotic and abiotic surfaces using their outer membrane proteins. Trimeric autotransporter adhesins (TAAs) are modular homotrimers of various length and domain complexity. They are a diverse, and widespread gene family constituting the type Vc secretion pathway. These adhesins have been established as virulence factors in Brucellaceae . To date, no comprehensive and exhaustive study has been performed on the trimeric autotransporter family in the genus. In the present study, various bioinformatics tools were used to provide a novel evolutionary insight into the sequence and structure of this protein family in Brucellaceae . To this end, a dataset of all trimeric autotransporters from the Brucella genomes was built. Analyses included but were not limited to sequence alignment, phylogenetic tree constructions, codon-based test for selection, clustering of the sequences, and structure (primary to quaternary) predictions. Batch analyzes of the dataset suggested the existence of a few structural domains within the whole population. BatA from the B. abortus 2308 genome was selected as a reference to describe the features of these structural domains. Furthermore, we examined the structural basis for the observed rigidity and resiliency of the protein structure through a molecular dynamics evaluation, which led us to deduce that the random drift results in the non-adaptive evolution of the trimeric autotransporter genes in the Brucella genus. Notably, the modifications have occurred across the genus without interference of gene transmission.

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Recruitment of Vitronectin by Bacterial Pathogens: A Comprehensive Overview

Pellegrini,

Pietrocola

2024

Microorganisms

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The key factor that enables pathogenic bacteria to establish successful infections lies largely in their ability to escape the host’s immune response and adhere to host surfaces. Vitronectin (Vn) is a multidomain glycoprotein ubiquitously present in blood and the extracellular matrix of several tissues, where it plays important roles as a regulator of membrane attack complex (MAC) formation and as a mediator of cell adhesion. Vn has emerged as an intriguing target for several microorganisms. Vn binding by bacterial receptors confers protection from lysis resulting from MAC deposition. Furthermore, through its Arg-Gly-Asp (RGD) motif, Vn can bind several host cell integrins. Therefore, Vn recruited to the bacterial cell functions as a molecular bridge between bacteria and host surfaces, where it triggers several host signaling events that could promote bacterial internalization. Each bacterium uses different receptors that recognize specific Vn domains. In this review, we update the current knowledge of Vn receptors of major bacterial pathogens, emphasizing the role they may play in the host upon Vn binding. Focusing on the structural properties of bacterial proteins, we provide details on the residues involved in their interaction with Vn. Furthermore, we discuss the possible involvement of Vn adsorption on biomaterials in promoting bacterial adhesion on abiotic surfaces and infection.

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Correction to: Binding of Brucella protein, Bp26, to select extracellular matrix molecules

Abstract: Following publication of the original article [1], an error was reported in the tagging of Eugene H. Johnson and Remya R. Nair in the author group.

Cited by 3 publications

References 1 publication

Recruitment of Vitronectin by Bacterial Pathogens: A Comprehensive Overview

Recruitment of Vitronectin by Bacterial Pathogens: A Comprehensive Overview

Non-adaptive Evolution of Trimeric Autotransporters in Brucellaceae

Recruitment of Vitronectin by Bacterial Pathogens: A Comprehensive Overview

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