Hsps (Heat Shock Proteins) also known as "molecular chaperones." are highly conserved across species and known for its key roles in cellular activities such as protein translocation, folding, and assembly. Major Hsp families consists of Hsp60, Hsp70, Hsp90, Hsp100, Hsp110 and small Hsps or sHsps (mol wt. < 40kDa) Hsp70 release into extracellular compartments has noticeable impacts on APCs for peptides absorption by MHCs. They often take up the role of “danger signals” Hsp synthesis, both constitutively expressed [heat shock cognates (Hscs)] and more usually not, upon protein denaturation stimulation. Hsp families establish an intracellular networks consisting of chaperones, co-chaperones, and accessory proteins for hsp to act together. For eg- Hsp90 Dimeric protein; an amino-terminal domain of individual monomeric protein for ATP hydrolysis co-chaperons interaction with -COO (carboxylic) domains. substrate binding by a middle domain Hsp families establish an intracellular networks consisting of chaperones, co-chaperones, and accessory proteins for hsp to act together. For eg- Hsp90 Dimeric protein; an amino-terminal domain of individual monomeric protein for ATP hydrolysis co-chaperons interaction with -COO (carboxylic) domains.   substrate binding by a middle domain Hsp families establish an intracellular networks consisting of chaperones, co-chaperones, and accessory proteins for hsp to act together. For eg- Hsp90 Dimeric protein; an amino-terminal domain of individual monomeric protein for ATP hydrolysis co-chaperons interaction with -COO (carboxylic) domains. substrate binding by a middle domain RESPONSE OF AQUATIC ORGANISMS TO DISEASE THROUGH HSP SYNTHESIS ALTERATION Penaeus monodon (Black tiger shrimp) upon challenge with V. harveyi (heat-killed ) in gills results in synthesis of Hsp90, Hsp70, Hsp21 Encounter of nodavirus by Epinephelus coioides ( orange-spotted grouper); involving virus-induced Hsp synthesis in fish, leads to an increase in Hsp90 Disease Management Approach In Aquatic Organisms By Increasing Hsps Heat shock- Hsp70 Hsp synthesis by exposure to chemical inducers- PRO-TEX Exogenous Hsps Administration Extracellular Hsps facilitated cell surface synthesis of peptides, support in distressed cells identification by the immune system “Danger signals” such as monocytes, dendrites, neutrophils, and macrophages are transmitted to immune cells by Hsp70 via TLR2 and TLR4 activation Stimulates inflammatory cytokines, nitric oxide (NO) synthase, NO, tumor necrosis factor-alpha (TNF-, Interleukin1-beta (IL-1, and IL-6) production Hsps may play a key role during adaptive immunity during Ag presentation by arranging MHC-peptide complexes into an assembly along with T lymphocytes activation for destroying or coordinating pathogen death and infections as well as cells that are not functional anymore Exploitation of pathogen derived Hsps that takes the role of prominent antigen.

2. Hsps (Heat Shock Proteins) also known as "molecular
chaperones." are highly conserved across species and known for its key
roles in cellular activities such as protein translocation, folding, and
assembly.
Major Hsp families consists of Hsp60, Hsp70, Hsp90, Hsp100, Hsp110 and
small Hsps or sHsps (mol wt. < 40kDa)
Hsp70 release into extracellular compartments has noticeable impacts on
APCs for peptides absorption by MHCs. They often take up the role of
“danger signals”
Hsp synthesis, both constitutively expressed [heat shock cognates (Hscs)]
and more usually not, upon protein denaturation stimulation.

3.  Hsp families establish an
intracellular networks
consisting of chaperones,
co-chaperones, and
accessory proteins for hsp to
act together.
For eg- Hsp90
•Dimeric protein; an amino-
terminal domain of individual
monomeric protein for ATP
hydrolysis co-chaperons
interaction with
-COO (carboxylic) domains.
•substrate binding by a
middle domain

4. •Penaeus monodon (Black tiger shrimp) upon challenge with V. harveyi
(heat-killed ) in gills results in synthesis of Hsp90, Hsp70, Hsp21
•Encounter of nodavirus by Epinephelus coioides ( orange-spotted
grouper); involving virus-induced Hsp synthesis in fish, leads to an
increase in Hsp90
•Disease Management Approach In Aquatic Organisms By Increasing Hsps
1. Heat shock- Hsp70
2. Hsp synthesis by exposure to chemical inducers- PRO-TEX
3. Exogenous Hsps Administration

6. Extracellular Hsps facilitated cell surface synthesis of peptides, support in
distressed cells identification by the immune system “Danger signals” such
as monocytes, dendrites, neutrophils, and macrophages are transmitted to
immune cells by Hsp70 via TLR2 and TLR4 activation
Stimulates inflammatory cytokines, nitric oxide (NO) synthase, NO, tumor
necrosis factor-alpha (TNF-, Interleukin1-beta (IL-1, and IL-6) production
 Hsps may play a key role during adaptive immunity during Ag
presentation by arranging MHC-peptide complexes into an assembly along
with T lymphocytes activation for destroying or coordinating pathogen death
and infections as well as cells that are not functional anymore

7.  Exploitation of pathogen derived Hsps that takes the role of
prominent antigen in numerous microbial diseases for the
development of vaccines to fight bacterial pathogens in fishes
is achieved by cDNAs cloning encoding hsps pathogen,
followed by their over-expression in bacteria, and purification
before their introduction into the host species.
 Proteins fused involving ISAV (Infectious Salmon Anemia
Virus) protein subunits and Hsps (Fishes) are still under
ongoing studies for the manufacture of new vaccines

8.  Compared to current approaches, Hsps are proved to be more
significant for curing diseases and other infections in the
species that are of commercial worth
 They are engaged in a wide range of biological and
immunological processes and exploited potentially for its
utilization in a wide range of therapeutic applications.
 Studies and researches conducted on Artemia depicted to be
promising for its protective functionalities.
 Hsps have potentially been exploited for the manufacture of
immune system-based therapies for life-threatening disorders
such as cancer and autoimmune diseases despite their
dangers.

9.  1. Morimoto, R. 1., Tissieres, A. and Georgopoulos, G. (1994) The
Biology of Heat Shock Proteins and Molecular Chaperones, Cold
Spring Harbor Laboratory Press
 2. Gething, M-J. and Sambrook. J. (1992) Nature 355, 33-45
 3. Ellis, R. (1987) Nature 328, 378-379
 4. Pockley AG (2003) Heat shock proteins as regulators of the
immune response. Lancet 362: 469-476.
 5. Sung YY, MacRae TH (2011) Heat shock proteins and disease
control in aquatic organisms. J Aquacult Res Dev S2: 006.