Cloning and expression pattern of a heat shock cognate protein 70 gene in ticks (Haemaphysalis flava)

Лю, Лэй; Cheng, Tao; Yang, Yaolong

doi:10.1007/s00436-017-5444-8

Cited by 12 publications

(7 citation statements)

References 28 publications

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“…These proteins are involved in the folding of newly synthesized proteins and are traditionally called 70-kDa heat shock cognates (HSC70). However, the distinction between HSP70s and HSC70s remains unclear because of the occasional reports of “constitutive HSP70s,” especially from invertebrates 16 – 18 . These proteins were named “HSP70” because of their higher sequence similarity to known HSP70s than to HSC70s, but subsequent expression analyses failed to demonstrate their stress inducibility, resulting in assignment of the apparently self-contradicting protein names.…”

Section: Introductionmentioning

confidence: 99%

The complex evolution of the metazoan HSP70 gene family

Yoshinaga

Jalufka

et al. 2021

Sci Rep

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The metazoan 70-kDa heat shock protein (HSP70) family contains several members localized in different subcellular compartments. The cytosolic members have been classified into inducible HSP70s and constitutive heat shock cognates (HSC70s), but their distinction and evolutionary relationship remain unclear because of occasional reports of “constitutive HSP70s” and the lack of cross-phylum comparisons. Here we provide novel insights into the evolution of these important molecular chaperones. Phylogenetic analyses of 125 full-length HSP70s from a broad range of phyla revealed an ancient duplication that gave rise to two lineages from which all metazoan cytosolic HSP70s descend. One lineage (A) contains a relatively small number of genes from many invertebrate phyla, none of which have been shown to be constitutively expressed (i.e., either inducible or unknown). The other lineage (B) included both inducible and constitutive genes from diverse phyla. Species-specific duplications are present in both lineages, and Lineage B contains well-supported phylum-specific clades for Platyhelminthes, Rotifera, Nematoda, Porifera/Cnidaria, and Chordata. Some genes in Lineage B have likely independently acquired inducibility, which may explain the sporadic distribution of “HSP70” or “HSC70” in previous phylogenetic analyses. Consistent with the diversification history within each group, inducible members show lower purifying selection pressure compared to constitutive members. These results illustrate the evolutionary history of the HSP70 family, encouraging us to propose a new nomenclature: “HSP70 + subcellular localization + linage + copy number in the organism + inducible or constitutive, if known.” e.g., HSP70cA1i for cytosolic Lineage A, copy 1, inducible.

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Section: Introductionmentioning

confidence: 99%

The complex evolution of the metazoan HSP70 gene family

Yoshinaga

Jalufka

et al. 2021

Sci Rep

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“…Two heat shock proteins 70 (HSP70) were found in tick hemolymph, and their expression was significantly upregulated upon blood-feeding [ 76 , 77 ]. HSP70-8 and HSC70 were shown to exert an anticoagulation effect in vitro [ 78 ].…”

Section: Resultsmentioning

confidence: 99%

Protein profiling of hemolymph in Haemaphysalis flava ticks

et al. 2022

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Background Tick hemolymph bathes internal organs, acts as an exchange medium for nutrients and cellular metabolites, and offers protection against pathogens. Hemolymph is abundant in proteins. However, there has been limited integrated protein analysis in tick hemolymph thus far. Moreover, there are difficulties in differentiating tick-derived proteins from the host source. The aim of this study was to profile the tick/host protein components in the hemolymph of Haemaphysalis flava. Methods Hemolymph from adult engorged H. flava females was collected by leg amputation from the Erinaceus europaeus host. Hemolymph proteins were extracted by a filter-aided sample preparation protocol, digested by trypsin, and assayed by liquid chromatography–tandem mass spectrometry (LC–MS/MS). MS raw data were searched against the UniProt Erinaceidae database and H. flava protein database for host- and tick-derived protein identification. Protein abundance was further quantified by intensity-based absolute quantification (iBAQ). Results Proteins extracted from hemolymph unevenly varied in size with intense bands between 100 and 130 kDa. In total, 312 proteins were identified in the present study. Therein 40 proteins were identified to be host-derived proteins, of which 18 were high-confidence proteins. Top 10 abundant host-derived proteins included hemoglobin subunit-α and subunit-β, albumin, serotransferrin-like, ubiquitin-like, haptoglobin, α-1-antitrypsin-like protein, histone H2B, apolipoprotein A-I, and C3-β. In contrast, 169 were high-confidence tick-derived proteins. These proteins were classified into six categories based on reported functions in ticks, i.e., enzymes, enzyme inhibitors, transporters, immune-related proteins, muscle proteins, and heat shock proteins. The abundance of Vg, microplusin and α-2-macroglobulin was the highest among tick-derived proteins as indicated by iBAQ. Conclusions Numerous tick- and host-derived proteins were identified in hemolymph. The protein profile of H. flava hemolymph revealed a sophisticated protein system in the physiological processes of anticoagulation, digestion of blood meal, and innate immunity. More investigations are needed to characterize tick-derived proteins in hemolymph. Graphical Abstract

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“…Liu et al . () compared mRNA abundance of HSC70 in different lifephases and engorgement levels of H. flava , finding that it was highest in partially‐engorged adult females. Vora et al .…”

Section: Discussionmentioning

confidence: 99%

“…Haemaphysalis flava , a member of the family Ixodidae, is widely distributed throughout Far East and East Asia (Chen et al ., 2010; Guglielmonee et al ., 2014). Its hosts include humans, dogs, ruminants, hedgehogs and giant pandas (Cheng et al ., ; Liu et al ., ). A variety of pathogens are detected in those ticks, such as encephalitis virus (Ko et al ., ), Rickettsiae spp.…”

Section: Introductionmentioning

confidence: 97%

Cloning of four HSPA multigene family members in Haemaphysalis flava ticks

Liu

et al. 2019

Medical Vet Entomology

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The heat shock protein 70 (HSPA) family and their genes have been studied in ticks and are considered as possible antigen candidates for the development of anti-tick vaccines. However, knowledge about their members, structure and function in ticks is incomplete. Based on our transcriptomic data, the full length of four HSPA genes in Haemaphysalis flava (Acari: Ixodidae) was cloned via rapid amplification of cDNA ends. The open reading frame of HSPA2A, HSPA2B, HSPA5 and HSPA9 was 1920, 1911, 1983 and 2088 bp in length, respectively. Three family signatures and one localization motif were in the encoding proteins. HSPA2A and HSPA2B were predicted to be located at cytoplasm/nucleus, whereas HSPA5 and HSPA9 were at endoplasmic reticulum and mitochondria, respectively. In silico simulation demonstrated that those proteins had distinct numbers of -helixes, extended strands and coils, and different antigenic epitopes. Expression of HSPA5 and HSPA9 in the salivary gland was significantly higher in partially-engorged female adult ticks than the fully-engorged (P < 0.01) as shown by a quantitative polymerase chain reaction. Our data indicated that H. flava ticks had at least four HSPA genes encoding proteins with different cellular locations, structures and expression profiles, suggesting their diverse roles in tick biology.

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Cloning and expression pattern of a heat shock cognate protein 70 gene in ticks (Haemaphysalis flava)

Cited by 12 publications

References 28 publications

The complex evolution of the metazoan HSP70 gene family

The complex evolution of the metazoan HSP70 gene family

Protein profiling of hemolymph in Haemaphysalis flava ticks

Cloning of four HSPA multigene family members in Haemaphysalis flava ticks

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