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Review
. 2019 Jun 19:10:588.
doi: 10.3389/fgene.2019.00588. eCollection 2019.

Cellular and Molecular Adaptation of Arabian Camel to Heat Stress

Abdullah Hoter  1   2 , Sandra Rizk  3 , Hassan Y Naim  2
Affiliations
Review

Cellular and Molecular Adaptation of Arabian Camel to Heat Stress

Abdullah Hoter et al. Front Genet. .

Abstract

To cope with the extreme heat stress and drought of the desert, the Arabian camel (Camelus dromedarius) has developed exceptional physiological and biochemical particularities. Previous reports focused mainly on the physiological features of Arabian camel and neglected its cellular and molecular characteristics. Heat shock proteins are suggested to play a key role in the protein homeostasis and thermotolerance. Therefore, we aim by this review to elucidate the implication of camel HSPs in its physiological adaptation to heat stress and compare them with HSPs in related mammalian species. Correlation of these molecules to the adaptive mechanisms in camel is of special importance to expand our understanding of the overall camel physiology and homeostasis.

Keywords: Arabian camel; adaptation; chaperones; desert; heat shock proteins; heat stress.

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Figures

FIGURE 1
FIGURE 1
Classification and distribution of camel species. The upper panel demonstrates the genera and species belonging to camelidae family. These include three genera, Camelus, Lama, and Vicugna, which comprise large camel species like Arabian camel (one humped camel) and Bactrian camel (two humped camel) as well as small camelids like llama, alpaca, guanaco and vicuna. Camelus ferus, which is a double humped wild Bactrian camel, is not shown for simplicity. The lower panel shows a visual distribution map of different species within camelidae family.
FIGURE 2
FIGURE 2
The main structural features of reported HSPs in Arabian camel. (A) Schematic representation of the HSP70 structural domains characterized from Camelus dromedarius. A list of identified HSP70 members in Arabian camel is shown on the right side. (B) The structural characteristics of HSPB proteins in Arabian camel. The reported protein sequences are highly homologous to their human peers and preserve the α-crystalline domain as well as the phosphorylation sites. (C) Structural topology of the reported HSP90 members in Arabian camel. The upper panel shows the cytoplasmic HSP90α while the lower panel reveals the ER localized GRP94. HSP90α differs from its ER paralog in lacking both the ER target and retention signals, instead it has a C-terminal MEEVD motif.
See this image and copyright information in PMC

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