Protein evolution of Toll-like receptors 4, 5 and 7 within Galloanserae birds

Vinkler, Michal; Bainová, Hana; Bryja, Josef

doi:10.1186/s12711-014-0072-6

Cited by 36 publications

(42 citation statements)

References 95 publications

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“…Although we are aware that our models are only predictions, given the structural conservatism in vertebrate TLRs and the high accuracy of our models, we consider them to be trustworthy. Together with similar results previously reported for nonpasserine birds and mammals (Fornůsková et al., ; Vinkler et al., ), our data thus indicate a high structural uniformity in TLRs, which appears to be an evolutionarily stable feature. In contrast (but again similar to nonpasserine birds and mammals; Fornůsková et al., ; Vinkler et al., ), TLR4 LBR surface charge distributions showed very distinct patterns across passerines, suggesting the importance of this physicochemical feature for ligand binding.…”

Section: Discussionsupporting

confidence: 91%

“…Given that six of these sites were at least in close topological proximity to sites also identified as positively selected, our data support the notion of this genetic variation having functional significance. Among the 34 sites detected in the passerine TLR4 LBR as positively selected based on the multiple criteria adopted in this study, ten have also been identified as positively selected in other avian studies (Alcaide & Edwards, ; Grueber et al., ; Vinkler et al., , ), and another eleven were consistent with sites previously detected as being under positive selection in both birds and mammals (Areal et al., ; Fornůsková et al., ; Grueber et al., ; Vinkler et al., , ; Wlasiuk & Nachman, ; for the consensual sites see Supporting Information Table ). This may suggest convergence in TLR4 molecular evolution among various vertebrate taxa.…”

Section: Discussionsupporting

confidence: 82%

“…Therefore, substitutions at this position altering the molecular charge from positive to negative may profoundly affect the recognition of diverse pathogens. Given that analogous positive selection has been shown in Galloanserae birds (Vinkler et al., ) and cyprinid fish (Tong et al., ), it appears likely that charge‐changing substitutions at position 267, which is directly involved in LPS and MD‐2 binding, may also be of particular evolutionary significance. Furthermore, the B‐cluster‐determining position 298, which was predicted to affect the receptor's secondary structure, has been identified as a positively selected site in mammals and birds (Areal et al., ; Vinkler et al., ; Wlasiuk & Nachman, ).…”

Section: Discussionmentioning

confidence: 76%

“…According to recent research in Galloanserae birds (Vinkler et al., ), one of the most important variable features of TLRs is the electrostatic potential distribution on the molecular surface, so we performed a closer examination of this property. To evaluate the anticipated functional differences in TLR4 LBRs between selected passerine species, we predicted the tertiary structure of each species‐specific protein using homology modelling tool modeller v. 9.14 (Eswar et al., ; pairwise sequence alignment performed in Geneious), with mouse TLR4 as a template with known crystal structure (Kim et al., ).…”

Section: Methodsmentioning

confidence: 99%

“…Substitutions in TLR4 can have either structural effects, changing the shape of the LBR or functional effects, for example altering surface molecular features such as its charge (Walsh et al., ). For example, in Galloanserae birds, the electrostatic potential distribution on the surface of the TLR4 molecule was found to be more significant than changes in tertiary structure (Vinkler et al., ).…”

Section: Introductionmentioning

confidence: 99%

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Signatures of diversifying selection and convergence acting on passerine Toll‐like receptor 4 in an evolutionary context

et al. 2018

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Positive selection acting on Toll-like receptors (TLRs) has been recently investigated to reveal evolutionary mechanisms of host-pathogen molecular co-adaptation. Much of this research, however, has focused mainly on the identification of sites predicted to be under positive selection, bringing little insight into the functional differences and similarities among species and a limited understanding of convergent evolution in the innate immune molecules. In this study, we provide evidence of phenotypic variability in the avian TLR4 ligand-binding region (LBR), the direct interface between host and pathogen molecular structures. We show that 55 passerine species vary substantially in the distribution of electrostatic potential on the surface of the receptor, and based on these distinct patterns, we identified four species clusters. Seven of the 34 evolutionarily nonconservative and positively selected residues correspond topologically to sites previously identified as being important for lipopolysaccharide, lipid IVa or MD-2 binding. Five of these positions codetermine the identity of the charge clusters. Groups of species that host-related communities of pathogens were predicted to cluster based on their TLR4 LBR charge. Despite some evidence for convergence among taxa, there were no clear associations between the TLR4 LBR charge distribution and any of the general ecological characteristics compared (migration, latitudinal distribution and diet). Closely related species, however, mostly belonged to the same surface charge cluster indicating that phylogenetic constraints are key determinants shaping TLR4 adaptive evolution. Our results suggest that host innate immune evolution is consistent with Fahrenholz's rule on the cospeciation of hosts and their parasites.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 76%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Signatures of diversifying selection and convergence acting on passerine Toll‐like receptor 4 in an evolutionary context

et al. 2018

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Evolution of TLR5

Pinheiro

2021

Encyclopedia of Life Sciences

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TLR5 is an evolutionary conserved protein. Evidence so far shows that it emerged in a vertebrate ancestor and maintained its flagellin recognition function throughout evolution. The single TLR5 gene that was present in the vertebrates' ancestor was duplicated in the Actinopterygii lineage originating a short ECD only TLR5 (TLR5S). The single TLR5 again suffered a duplication in the tetrapoda ancestor originating another short ECD only TLR5 (TLR5L). This TLR5L was then independently lost in the Reptilia Archosauromorpha lineage, which comprises crocodiles and birds, and in the mammals' lineage, and is nowadays present only in Amphibians and most reptiles. TLR5 pseudogenisation events are common, with higher incidence in birds and mammals. These gene gains and losses may reflect species adaptation to particular environments and pathogens. It is also apparent that, in birds and mammals, TLR5 may be functionally redundant and is acquiring new functions beyond flagellin recognition. Key Concepts TLR5 is a vertebrate Toll‐like receptor that binds bacterial flagellin. TLR5 is overall an evolutionary conserved protein being present and maintaining its function from lampreys to mammals. The TLR5 evolution has been punctuated by several independent gene gains and losses, characteristic events of a multigene family evolution. In birds and mammals, the finding of positively selected codons suggests that TLR5 is evolving in response to pathogen pressure. Growing evidence suggests that TLR5 function may be redundant, and hence, the gene has been lost or pseudogenised in many birds and mammals.

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Adaptive evolution of virus-sensing toll-like receptor 8 in bats

Schad

Voigt

2016

Immunogenetics

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Recently, bats have gained attention as potential reservoir hosts for emerging zoonotic single-stranded (ssRNA) viruses that may prove fatal for humans and other mammals. It has been hypothesized that some features of their innate immune system may enable bats to trigger an efficient early immune response. Toll-like receptors (TLRs) represent a first line defense within the innate immune system and lie directly at the host-pathogen interface in targeting specific microbe-molecular patterns. However, the direction and strength of selection acting on TLRs are largely unknown for bats. Here, we studied the selection on viral ssRNA sensing TLR8 based on sequence data of 21 bat species. The major part (63 %) of the TLR8 gene evolved under purifying selection, likely due to functional constraints. We also found evidence for persistent positive selection acting on specific amino acid sites (7 %), especially when compared to viral TLR evolution of other mammals. All of these putatively positively selected codons were located in the ligand-binding ectodomain, some coincidenced or were in close proximity to functional sites, as suggested by the crystallographic structure of the human TLR8. This might contribute to the inter-species variation in the ability to recognize molecular patterns of viruses. TLR8 evolution within bats revealed that branches leading to ancestral and recent lineages evolved under episodic positive selection, indicating selective selection pressures in restricted bat lineages. Altogether, we found that the TLR8 displays extensive sequence variation within bats and that unique features separate them from humans and other mammals.

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Protein evolution of Toll-like receptors 4, 5 and 7 within Galloanserae birds

Cited by 36 publications

References 95 publications

Signatures of diversifying selection and convergence acting on passerine Toll‐like receptor 4 in an evolutionary context

Signatures of diversifying selection and convergence acting on passerine Toll‐like receptor 4 in an evolutionary context

Evolution of TLR5

Adaptive evolution of virus-sensing toll-like receptor 8 in bats

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