scholarly journals Oyster heat shock protein 70 plays a role in binding of human noroviruses

2021 ◽  
Author(s):  
Zilei Zhang ◽  
Danlei Liu ◽  
Qingping Wu ◽  
Dapeng Wang
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Specific Binding ◽  
Surface Display ◽  
Cell Surface Display ◽  
Enzyme Linked Immunosorbent Assay ◽  
Oyster Tissue ◽  
Human Noroviruses ◽  
Viral Particles

Human noroviruses (HuNoVs) are important foodborne pathogens causing acute gastroenteritis. Oysters are an important vehicle for transmission of HuNoVs. Histo-blood group antigen (HBGA)-like substances are considered the primary ligands for bioaccumulation of HuNoVs in oyster tissues. In this study, proteinaceous ligands for specific binding of HuNoVs were mined from oyster tissues using a bacterial cell surface display system. The macromolecular target was captured and identified in proteomic analysis. The distribution of viral particles, oyster heat shock protein 70 (oHSP 70), and type A HBGA (positive control) in oyster tissue was investigated by multiplex immunofluorescence assays after artificial contamination with HuNoVs (GII.4). Our results demonstrated that oHSP 70 is a candidate vital ligand for specific binding of HuNoVs in oyster tissues. In addition, P proteins (GI.1 and GII.4) and viral particles (GI.1 and GII.4) were captured by recombinant oHSP 70 in an enzyme-linked immunosorbent assay with sample signal/negative signal of 7.8, 6.3, 17.0, and 8.8, respectively. The findings suggested that oHSP 70 plays an important role in the binding of these foodborne viruses. Importance Human noroviruses (HuNoVs) are the most important pathogen for non-bacterial epidemic gastroenteritis cases. Foodborne transmission plays an important role in HuNoVs infection. Oysters, filter-feeding epibenthic bivalves, can be contaminated by faecal discharge in harvest water. A new proteinaceous ligand for HuNoVs other than HBGA is identified in oyster tissues. The significance of our research is in identifying and verifying the ligands in oyster tissues for HuNoVs binding. Our data will allow a better understanding of HuNoVs attachment and transmission with oysters, leading to control of undesired foodborne disease.

scholarly journals Cell Surface-bound Heat Shock Protein 70 (Hsp70) Mediates Perforin-independent Apoptosis by Specific Binding and Uptake of Granzyme B

2003 ◽  
Vol 278 (42) ◽  
pp. 41173-41181 ◽  
Author(s):  
Catharina Gross ◽  
Walter Koelch ◽  
Antonio DeMaio ◽  
Nelson Arispe ◽  
Gabriele Multhoff
Keyword(s):  
Heat Shock ◽  
Cell Surface ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Specific Binding ◽  
Granzyme B

Relationship between heat shock protein 70 and B amyloids in patients with alzheimer disease and vascular dementia

2011 ◽  
Vol 26 (S2) ◽  
pp. 505-505
Author(s):  
Y. Fu ◽  
S. Xiao
Keyword(s):  
Heat Shock ◽  
Alzheimer Disease ◽  
Heat Shock Protein ◽  
Vascular Dementia ◽  
Heat Shock Protein 70 ◽  
High Plasma ◽  
Enzyme Linked Immunosorbent Assay ◽  
Statistical Manual ◽  
The Relationship ◽  
Normal Controls

AimsExplore the relationship between levels of plasma Aβ1–40, Aβ1–42 and heat shock protein 70 (HSP70) in patients with Alzheimer disease (AD) and vascular dementia (VD) and in elderly non-demented controls.Methods23 patients with AD and 21 patients with VD who meet diagnostic criteria of the Diagnostic Statistical Manual 4th edition and 20 control subjects were enrolled, administered the Mini-Mental State Exam (MMSE) and the Activity of Daily Living (ADL) inventory and their levels of plasma Aβ1–40, Aβ1–42 and HSP70 were measured by sandwich enzyme-linked immunosorbent assay.ResultsThe levels of plasma Aβ1–40, Aβ1–42 and the Aβ1–40/Aβ1–42 ratio were not significantly different across groups, but levels of plasma HSP70 in VD patients was significantly higher than in AD patients and in normal controls (3.19 vs 1.91 vs 1.43ng/ml, respectively; F=6.464, P=0.003). In the AD group MMSE scores were inversely correlated with ADL scores (r=-0.617, P=0.002) and with levels of plasma HSP70 (r=-0.437, P=0.037); but HSP70 levels were positively correlated with age (r=0.616, P=0.002) and with plasma Aβ1–40 (r=0.497, P=0.016) in AD group. In the VD group levels of plasma HSP70 were positively correlated with plasma Aβ1–40 (r=0.436, P=0.048).ConclusionsOur findings provide further evidence that high plasma HSP70 levels may play a role in the diagnosis and differential diagnosis of AD. HSP70 levels in AD patients is inversely associated with cognitive performance and positively correlated with plasma Aβ1–40. Plasma HSP70 in VD patients is significantly elevated and positively correlated with plasma Aβ1–40.

scholarly journals Heat Shock Protein 70 and Anti-heat Shock Protein 70 Antibodies in Nasal Secretions of Patients with Chronic Rhinosinusitis

2016 ◽  
Vol 7 (1) ◽  
pp. ar.2016.7.0149 ◽  
Author(s):  
Namjil N. Tsybikov ◽  
Elena V. Egorova ◽  
Boris I. Kuznik ◽  
Elena V. Fefelova ◽  
Eli Magen
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Chronic Rhinosinusitis ◽  
Heat Shock Protein 70 ◽  
Nasal Polyps ◽  
Immunoglobulin E ◽  
Clinical Severity ◽  
Secretory Iga ◽  
Enzyme Linked Immunosorbent Assay ◽  
Antibody Levels

Background The issue of heat shock protein (HSP) 70 and anti-HSP70 antibodies in chronic rhinosinusitis (CRS) has never been explored. Objective To determine the nasal secretion (NS) levels of HSP70 and anti-HSP70 antibodies in patients with CRS with nasal polyps (CRSwNP) and patients with CRS without nasal polyps (CRSsNP), and to evaluate their associations with CRS clinical severity and correlation with NS interleukin (IL), IL-5 and interferon λ. Methods CRS severity was determined by Lund-Mackay scores. Levels of immunoglobulin E (IgE), IL-4, IL-5, interferon A, HSP70, and anti-HSP70 antibody levels in NS were measured by enzyme-linked immunosorbent assay. Results Forty-six patients with CRSsNP (25 women [543%] and 21 men [45.7%], mean [standard deviation {SD}]) age, 34.1 ± 123 years; 54 patients with CRSwNP (24 women [44.4%] and 30 men [55.6%], mean [SD] age, 37.9 ± 17.5 years). A group of 40 healthy subjects served as controls. Compared with the controls (with a mean [SD] NS HSP70 level of 0.05 ± 0.03 μg/mL), mean [SD]NS HSP70 levels in both the CRSsNP group (0.16 ± 0.07 ixg/mL) and CRSwNP group (0.21 ± 0.10 μg/mL) were increased (p < 0.001). Similarly, the mean (SD) NS anti-HSP70 antibody levels were significantly higher in patients with CRSwNP (0.25 ± 0.09 optical density value [ODV]) compared with CRSsNP (0.13 ± 0.04 ODV) (p < 0.001) and healthy controls (0.14 ± 0.02 ODV) (p < 0.001). NS HSP70 in subjects with CRSwNP showed a significant positive correlation with the Lund-Mackay score (r = 0.31; p < 0.05). NS levels of either HSP70 or anti-HSP70 antibodies were strongly correlated with NS IL-4 in the CRSwNP group (r = 0.62, p < 0.001; and r = 0.69, p < 0.001, respectively). Conclusion NS concentrations of HSP70 and secretory IgA anti HSP70 antibodies are increased in CRSwNP (but not in CRSsNP) and correlate positively with the Lund-Mackay score, NS IL-4, and NS IL-5.

Inhibition of heat shock protein 70 blocks the development of cardiac hypertrophy by modulating the phosphorylation of histone deacetylase 2

2018 ◽  
Vol 115 (13) ◽  
pp. 1850-1860 ◽  
Author(s):  
Somy Yoon ◽  
Mira Kim ◽  
Hyun-Ki Min ◽  
Yeong-Un Lee ◽  
Duk-Hwa Kwon ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cardiac Hypertrophy ◽  
Histone Deacetylase ◽  
Heat Shock Protein 70 ◽  
Specific Binding ◽  
Primary Cultures ◽  
Histone Deacetylase 2 ◽  
Ventricular Cardiomyocytes

Abstract Aims Previously, we reported that phosphorylation of histone deacetylase 2 (HDAC2) and the resulting activation causes cardiac hypertrophy. Through further study of the specific binding partners of phosphorylated HDAC2 and their mechanism of regulation, we can better understand how cardiac hypertrophy develops. Thus, in the present study, we aimed to elucidate the function of one such binding partner, heat shock protein 70 (HSP70). Methods and results Primary cultures of rat neonatal ventricular cardiomyocytes and H9c2 cardiomyoblasts were used for in vitro cellular experiments. HSP70 knockout (KO) mice and transgenic (Tg) mice that overexpress HSP70 in the heart were used for in vivo analysis. Peptide-precipitation and immunoprecipitation assay revealed that HSP70 preferentially binds to phosphorylated HDAC2 S394. Forced expression of HSP70 increased phosphorylation of HDAC2 S394 and its activation, but not that of S422/424, whereas knocking down of HSP70 reduced it. However, HSP70 failed to phosphorylate HDAC2 in the cell-free condition. Phosphorylation of HDAC2 S394 by casein kinase 2α1 enhanced the binding of HSP70 to HDAC2, whereas dephosphorylation induced by the catalytic subunit of protein phosphatase 2A (PP2CA) had the opposite effect. HSP70 prevented HDAC2 dephosphorylation by reducing the binding of HDAC2 to PP2CA. HSP70 KO mouse hearts failed to phosphorylate S394 HDAC2 in response to isoproterenol infusion, whereas Tg overexpression of HSP70 increased the phosphorylation and activation of HDAC2. 2-Phenylethynesulfonamide (PES), an HSP70 inhibitor, attenuated cardiac hypertrophy induced either by phenylephrine in neonatal ventricular cardiomyocytes or by aortic banding in mice. PES reduced HDAC2 S394 phosphorylation and its activation by interfering with the binding of HSP70 to HDAC2. Conclusion These results demonstrate that HSP70 specifically binds to S394-phosphorylated HDAC2 and maintains its phosphorylation status, which results in HDAC2 activation and the development of cardiac hypertrophy. Inhibition of HSP70 has possible application as a therapeutic.

Cognitive Function and Heat Shock Protein 70 in Children With Temporal Lobe Epilepsy

2016 ◽  
Vol 32 (1) ◽  
pp. 41-45 ◽  
Author(s):  
Azza M. Oraby ◽  
Ehab R. Abdol Raouf ◽  
Mostafa M. El-Saied ◽  
Maha K. Abou-Khadra ◽  
Suzette I. Helal ◽  
...  
Keyword(s):  
Cognitive Function ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Temporal Lobe Epilepsy ◽  
Temporal Lobe ◽  
Heat Shock Protein 70 ◽  
Short Term Memory ◽  
Enzyme Linked Immunosorbent Assay ◽  
Control Group ◽  
Composite Scores

We conducted the present study to examine cognitive function and serum heat shock protein 70 levels among children with temporal lobe epilepsy. The Stanford-Binet Intelligence Test was carried out to examine cognitive function in 30 children with temporal lobe epilepsy and 30 controls. Serum heat shock protein 70 levels were determined with an enzyme-linked immunosorbent assay. The epilepsy group had significantly lower cognitive function testing scores and significantly higher serum heat shock protein 70 levels than the control group; there were significant negative correlations between serum heat shock protein 70 levels and short-term memory and composite scores. Children with uncontrolled seizures had significantly lower verbal reasoning scores and significantly higher serum heat shock protein 70 levels than children with controlled seizures. Children with temporal lobe epilepsy have cognitive dysfunction and elevated levels of serum heat shock protein 70, which may be considered a stress biomarker.

scholarly journals Serum heat shock protein 70 levels as a biomarker for inflammatory processes in multiple sclerosis

2018 ◽  
Vol 4 (2) ◽  
pp. 205521731876719 ◽  
Author(s):  
Patricia Lechner ◽  
Dorothea Buck ◽  
Lisa Sick ◽  
Bernhard Hemmer ◽  
Gabriele Multhoff
Keyword(s):  
Multiple Sclerosis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Neurological Diseases ◽  
Serum Levels ◽  
Enzyme Linked Immunosorbent Assay ◽  
Serum Samples ◽  
Potential Biomarker ◽  
Inflammatory Processes

Background Inflammatory and neurodegenerative processes are hallmarks of multiple sclerosis (MS). The synthesis of the major stress-inducible heat shock protein 70 (Hsp70) is induced by inflammation. Objective The purpose of this study is to determine whether Hsp70 in serum can serve as a potential biomarker to distinguish inflammatory and neurodegenerative processes in MS. Methods Serum was obtained from 94 patients: 26 clinically isolated syndrome (CIS), 40 relapsing–remitting MS (RRMS), 19 secondary progressive MS (SPMS), and nine primary progressive MS (PPMS). As controls, serum samples were collected from patients with non-inflammatory neurological diseases (NINDs, n = 41), other inflammatory neurological diseases (OINDs, n = 28) and healthy donors (HDs, n = 114). Serum levels of Hsp70 were quantified using the enzyme-linked immunosorbent assay detecting free and liposomal Hsp70 (lipHsp70 ELISA). Results Patients with MS displayed significantly higher Hsp70 serum levels than HDs ( p < 0.001) and significantly lower levels than OINDs ( p = 0.001). A subgroup analysis revealed that Hsp70 serum levels of CIS/RRMS patients are significantly higher than those of patients with progressive MS (SPMS/PPMS) ( p < 0.05). Conclusion Inflammation causes the release of Hsp70 into the blood. As CIS/RRMS are associated with higher Hsp70 serum levels than progressive MS, serum Hsp70 levels might provide a marker for inflammatory processes.

An enzyme‐linked immunosorbent assay for heat‐shock protein 70 in plants

1991 ◽  
Vol 3 (1) ◽  
pp. 29-36 ◽  
Author(s):  
K. G. Adham ◽  
M. C. Wilkinson ◽  
C. J. Smith ◽  
D. L. Laidman
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Immunosorbent Assay ◽  
Heat Shock Protein 70 ◽  
Enzyme Linked Immunosorbent Assay

scholarly journals Detection of Humoral Response Using a Recombinant Heat Shock Protein 70, DnaK, of Mycoplasma haemofelis in Experimentally and Naturally Hemoplasma-Infected Cats

2010 ◽  
Vol 17 (12) ◽  
pp. 1926-1932 ◽  
Author(s):  
Emily N. Barker ◽  
Chris R. Helps ◽  
Kate J. Heesom ◽  
Christopher J. Arthur ◽  
Iain R. Peters ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Western Blotting ◽  
Heat Shock Protein 70 ◽  
Acute Infection ◽  
Amino Acid Sequences ◽  
Mass Spectrometry Data ◽  
Clinical Samples ◽  
Enzyme Linked Immunosorbent Assay ◽  
Two Dimensional Gel Electrophoresis

ABSTRACT Hemoplasmas is the trivial name given to a group of erythrocyte-parasitizing bacteria of the genus Mycoplasma. Of the feline hemoplasmas, Mycoplasma haemofelis is the most pathogenic, while “Candidatus Mycoplasma haemominutum” and “Candidatus Mycoplasma turicensis” are less pathogenic. Shotgun libraries of fragmented M. haemofelis genomic DNA were constructed, and random colonies were selected for DNA sequencing. In silico-translated amino acid sequences of putative open reading frames were compared to mass spectrometry data from M. haemofelis protein spots identified as being immunogenic by two-dimensional gel electrophoresis and Western blotting. Three of the spots matched the predicted sequences of a heat shock protein 70 (DnaK) homolog, elongation factor Ts, and a fragment of phosphoglycerate kinase found during library screening. A full-length copy of the M. haemofelis dnaK gene was cloned into Escherichia coli and recombinantly expressed. Recombinant M. haemofelis DnaK was purified and then used in Western blotting and an enzyme-linked immunosorbent assay (ELISA) to investigate the humoral immune response during acute infection in cats experimentally infected with M. haemofelis, “Ca. Mycoplasma haemominutum,” or “Ca. Mycoplasma turicensis”. The recombinant M. haemofelis DnaK ELISA also was used to screen clinical samples submitted for hemoplasma PCR testing to a commercial laboratory (n = 254). Experimentally infected cats became seropositive following infection, with a greater and earlier antibody response seen in cats inoculated with M. haemofelis than those seen in cats inoculated with “Ca. Mycoplasma haemominutum” or “Ca. Mycoplasma turicensis,” by both Western blotting and ELISA. Of the clinical samples, 31.1% had antibodies detected by the ELISA but only 9.8% were positive by PCR for one or more hemoplasmas.

Sign in / Sign up

Export Citation Format

Share Document