Structural analysis of <i>Borrelia burgdorferi</i> periplasmic lipoprotein <scp>BB</scp>0365 involved in Lyme disease infection

Brangulis, K.; Akopjana, Ināra; Petrovskis, Ivars; Kazāks, Andris; Jekabsons, Atis; Jaudzems, Kristaps; Vīksna, Artūrs; Bērtiņš, Māris; Tars, K.

doi:10.1002/1873-3468.13594

Cited by 4 publications

(1 citation statement)

References 53 publications

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“…LA7 may, therefore, be important for spirochete survival in feeding arthropods. A recent analysis of the high-resolution structure of LA7 will likely contribute to our understanding of the biological function of the protein (Brangulis et al, 2020a).…”

Section: La7mentioning

confidence: 99%

Interactions Between Ticks and Lyme Disease Spirochetes

Pal¹,

Kitsou²,

Drecktrah³

et al. 2022

Current Issues in Molecular Biology

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Borrelia burgdorferi sensu lato causes Lyme borreliosis in a variety of animals and humans. These atypical bacterial pathogens are maintained in a complex enzootic life cycle that primarily involves a vertebrate host and Ixodes spp. ticks. In the Northeastern United States, I. scapularis is the main vector, while wild rodents serve as the mammalian reservoir host. As B. burgdorferi is transmitted only by I. scapularis and closely related ticks, the spirochete-tick interactions are thought to be highly specific. Various borrelial and arthropod proteins that directly or indirectly contribute to the natural cycle of B. burgdorferi infection have been identified. Discrete molecular interactions between spirochetes and tick components also have been discovered, which often play critical roles in pathogen persistence and transmission by the arthropod vector. This review will focus on the past discoveries and future challenges that are relevant to our understanding of the molecular interactions between B. burgdorferi and Ixodes ticks. This information will not only impact scientific advancements in the research of ticktransmitted infections but will also contribute to the development of novel preventive measures that interfere with the B. burgdorferi life cycle. caister.com/cimb 113 Curr. Issues Mol. Biol. Vol. 42 Curr. Issues Mol. Biol. 42: 113-144. caister.com/cimb Interactions Between Ticks and Spirochetes Pal et al.scapularis are highly specific. Limited studies have shed light on these complex pathogen-tick interactions (Munderloh and Kurtti, 1995;Fikrig and Narasimhan, 2006); a recent review summarizes our most current state of knowledge about the interactions between B. burgdorferi and I. scapularis ticks (Kurokawa et al., 2020). Vector competence, which depends on genetic determinants influencing the vector's ability to transmit a pathogen, also shapes interactions involving the tick, pathogen, and host (de la Fuente et al., 2017). With the advent of genetic tools for creating Borrelia mutants (Samuels et al., 2018) (see also Radolf and Samuels, 2021) and the current availability of the I. scapularis genome (Gulia-Nuss et al., 2016;Miller et al., 2018), investigators will have increasingly robust tools for studying Borrelia-tick interactions, both during the arthropod phase of the spirochete life cycle and at the interface with the mammalian host. A few borrelial proteins already have been demonstrated as prerequisites for spirochete-vector interactions, particularly with receptors in select tick organs, such as the gut or salivary gland (

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Section: La7mentioning

confidence: 99%

Interactions Between Ticks and Lyme Disease Spirochetes

Pal¹,

Kitsou²,

Drecktrah³

et al. 2022

Current Issues in Molecular Biology

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The surface lipoproteins of gram-negative bacteria: Protectors and foragers in harsh environments

Cole

Bateman

Moraes

2021

Journal of Biological Chemistry

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Gram-negative pathogens are enveloped by an outer membrane that serves as a double-edged sword: On the one hand, it provides a layer of protection for the bacterium from environmental insults, including other bacteria and the host immune system. On the other hand, it restricts movement of vital nutrients into the cell and provides a plethora of antigens that can be detected by host immune systems. One strategy used to overcome these limitations is the decoration of the outer surface of gram-negative bacteria with proteins tethered to the outer membrane through a lipid anchor. These surface lipoproteins (SLPs) fulfill critical roles in immune evasion and nutrient acquisition, but as more bacterial genomes are sequenced, we are beginning to discover their prevalence and their different roles and mechanisms and importantly how we can exploit them as antimicrobial targets. This review will focus on representative SLPs that gram-negative bacteria use to overcome host innate immunity, specifically the areas of nutritional immunity and complement system evasion. We elaborate on the structures of some notable SLPs required for binding target molecules in hosts and how this information can be used alongside bioinformatics to understand mechanisms of binding and in the discovery of new SLPs. This information provides a foundation for the development of therapeutics and the design of vaccine antigens.

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Controlled Proteolysis of an Essential Virulence Determinant Dictates Infectivity of Lyme Disease Pathogens

et al. 2022

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The Borrelia burgdorferi BB0323 protein undergoes a complex yet poorly defined proteolytic maturation event that generates N-terminal and C-terminal proteins with essential functions in cell growth and infection. Here, we report that a borrelial protease, B. burgdorferi high temperature requirement A protease (BbHtrA), cleaves BB0323 between asparagine (N) and leucine (L) at positions 236 and 237, while the replacement of these residues with alanine in the mutant protein prevents its cleavage, despite preserving its normal secondary structure.

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Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection

Cited by 4 publications

References 53 publications

Interactions Between Ticks and Lyme Disease Spirochetes

Interactions Between Ticks and Lyme Disease Spirochetes

The surface lipoproteins of gram-negative bacteria: Protectors and foragers in harsh environments

Controlled Proteolysis of an Essential Virulence Determinant Dictates Infectivity of Lyme Disease Pathogens

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