The role of small heat shock proteins in parasites

Pérez-Morales, Deyanira; Espinoza, Bertha

doi:10.1007/s12192-015-0607-y

Cited by 48 publications

(26 citation statements)

References 64 publications

(95 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Small-HSPs (sHSPs) are considered to be a crucial research focus in the fight against parasitic diseases [ 44 ]. sHSPs can induce an immune response in the host, thereby generating potential protection against the disease [ 44 ]. However, the information available about their role is still insufficient.…”

Section: Discussionmentioning

confidence: 99%

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

et al. 2017

View full text Add to dashboard Cite

BackgroundA wide range of molecules are used by tapeworm metacestodes to establish successful infection in the hostile environment of the host. Reports indicating the proteins in the cestode-host interactions are limited predominantly to taeniids, with no previous data available for non-taeniid species. A non-taeniid, Hymenolepis diminuta, represents one of the most important model species in cestode biology and exhibits an exceptional developmental plasticity in its life-cycle, which involves two phylogenetically distant hosts, arthropod and vertebrate.ResultsWe identified H. diminuta cysticercoid proteins that were recognized by sera of H. diminuta-infected rats using two-dimensional gel electrophoresis (2DE), 2D-immunoblotting, and LC-MS/MS mass spectrometry. Proteomic analysis of 42 antigenic spots revealed 70 proteins. The largest number belonged to structural proteins and to the heat-shock protein (HSP) family. These results show a number of the antigenic proteins of the cysticercoid stage, which were present already in the insect host prior to contact with the mammal host. These are the first parasite antigens that the mammal host encounters after the infection, therefore they may represent some of the molecules important in host-parasite interactions at the early stage of infection.ConclusionsThese results could help in understanding how H. diminuta and other cestodes adapt to their diverse and complex parasitic life-cycles and show universal molecules used among diverse groups of cestodes to escape the host response to infection.Electronic supplementary materialThe online version of this article (10.1186/s13071-017-2519-4) contains supplementary material, which is available to authorized users.

show abstract

Section: Discussionmentioning

confidence: 99%

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

et al. 2017

View full text Add to dashboard Cite

show abstract

“…However, there are still some common characteristics in the structure and function of sHSPs, which have a relatively conserved α‐crystalling domain spanning about 80∼100 amino acid residues, located near the C‐terminal region (Caspers et al ., ; Fu et al ., ; Perez‐Morales & Espinoza, ). In the secondary structure, sHSP monomers are enriched in β ‐strands organized in a β ‐sheet sandwich responsible for dimer formation (Sun & MacRae, ).…”

Section: Introductionmentioning

confidence: 99%

Characterization and functional analysis of hsp18.3 gene in the red flour beetle, Tribolium castaneum

Xie

Zhai

et al. 2017

Insect Science

View full text Add to dashboard Cite

Small heat shock proteins (sHSPs) are diverse and mainly function as molecular chaperones to protect organisms and cells from various stresses. In this study, hsp18.3, one Tribolium castaneum species-specific shsp, has been identified. Quantitative real-time polymerase chain reaction illustrated that Tchsp18.3 is expressed in all developmental stages, and is highly expressed at early pupal and late adult stages, while it is highly expressed in ovary and fat body at the adult period. Moreover, it was up-regulated 4532 ± 396-fold in response to enhanced heat stress but not to cold stress; meanwhile the lifespan of adults in ds-Tchsp18.3 group reduced by 15.8% from control group under starvation. Laval RNA interference (RNAi) of Tchsp18.3 caused 86.1% ± 4.5% arrested pupal eclosion and revealed that Tchsp18.3 played an important role in insect development. In addition, parental RNAi of Tchsp18.3 reduced the oviposition amount by 94.7%. These results suggest that Tchsp18.3 is not only essential for the resistance to heat and starvation stress, but also is critical for normal development and reproduction in T. castaneum.

show abstract

“…The reason for these phenomena is not yet clear, perhaps different organisms produced different types and quantities of shsps according to their varied behaviours during the long process of evolution (Li, Beeman, & Park, 2011). However, diverse and variable sHSPs still have the common characteristic with a conserved sequence of about 80-100 residues, the α-crystallin domain, located in the C-terminal region and folded into a β-sandwich conformation (Franck et al, 2004;Perez-Morales & Espinoza, 2015). Based on this conserved structure, it was discovered that the sHSPs of Drosophila melanogaster are evolutionarily related to the lens protein α-crystallin (Ingolia & Craig, 1982), and then, they are thought to have originated from a common ancestor.…”

mentioning

confidence: 99%

Characterization and functional analysis of hsp21.8b: An orthologous small heat shock protein gene in Tribolium castaneum

Xie

Xiong

et al. 2018

J Applied Entomology

View full text Add to dashboard Cite

Small heat shock proteins (sHSPs) act as molecular chaperones and are widely distributed in all kinds of organisms. Comparative analysis revealed that an orthologous shsp was present during insect evolution. Here, hsp21.8b, one insect orthologous shsp, had been identified in Tribolium castaneum. Quantitative real‐time PCR illustrated that Tchsp21.8b was expressed in all developmental stages, along with the lowest expression at early embryonic stage and relative high expression at other stages especially in late eggs and late pupae. In the adult period, Tchsp21.8b exhibited the highest expression level in central nervous system and followed in elytron, epidermis, ovary and fat body. Moreover, it was upregulated 3.39‐fold in response to enhanced heat stress (45°C) for 4 hr but not to cold stress (4°C) and was upregulated by 1.73‐ to 1.94‐fold under ultraviolet (UV) exposure during 4–6 hr. It was also downregulated by 20.8%–41.8% under starvation in 3 days and had a “down‐up‐down” trend under the pathogen stresses. Larval RNA interference of Tchsp21.8b caused 40.6% insects mortality and reduced the oviposition amount by 66.0% and only 21.0% of the ds‐Tchsp21.8b eggs could hatch into larvae. These results suggested that as an orthologous shsp, Tchsp21.8b not only plays important roles in the growth, development and fecundity of T. castaneum but with the competence to resist the environment stresses, although the response is relatively weak compared to other hsps. Results from this study also uncovered the functions of the orthologous shsp in the development and anti‐stresses ability of T. castanuem. It provided more scientific evidence for revealing the physiological mechanisms of shsps of the insects and enhanced the capabilities to control different pests.

show abstract

The role of small heat shock proteins in parasites

Cited by 48 publications

References 64 publications

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

Identification of immunogenic proteins of the cysticercoid of Hymenolepis diminuta

Characterization and functional analysis of hsp18.3 gene in the red flour beetle, Tribolium castaneum

Characterization and functional analysis of hsp21.8b: An orthologous small heat shock protein gene in Tribolium castaneum

Contact Info

Product

Resources

About