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PLoS One
2020 Sep 21;159:e0236724. doi: 10.1371/journal.pone.0236724.
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Aquaporin expression in the alimentary canal of the honey bee Apis mellifera L. (Hymenoptera: Apidae) and functional characterization of Am_Eglp 1.
Linhares Lino de Souza D
,
Serrão JE
,
Hansen IA
.
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Aquaporins (AQP) are a family of plasma membrane proteins responsible for water transport through cell membranes. They are differentially expressed in different parts of the alimentary canal of insects where they regulate water transport. These proteins have been studied in detail in some insects, but few data are available for aquaporins of the honey bee, Apis mellifera. We used quantitative PCR to study the expression of six putative aquaporin genes in forager honey bees. We found differential expression of all putative AQP genes in crop, midgut, ileum, rectum and Malpighian tubules. We found the entomoglyceroporin Am_Eglp 1 expressed at extremely high levels in the midgut. We performed a functional characterization of Am_Eglp 1 using heterologous expression in Xenopus laevis oocyte followed by water uptake assays. Our results confirmed that the Am_Eglp 1 gene encodes a functional water transporter. This study shows that all putative honey bee aquaporin genes have complex expression patterns in the digestive and excretory organs of honey bee workers. Our results suggest that Am_Eglp 1 is the principal water transporter in the midgut of A. mellifera workers.
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32956406
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Fig 1. Relative expression of aquaporins genes in the digestive tract and Malpighian tubules of A. mellifera forager workers.Shown are relative mRNA expression levels determined with qPCR. Values are means ± SD. Means separated by Tukeyâs range test (p<0.05). Means which share the same letter are not significantly different. MT: Malpighian tubules.
Fig 2. Sequence analyses of Am_Eglp 1.A: Amino acid sequence alignment of aquaporins from different organisms with different mercury (HgCl2) sensitivity. Am_Eglp 1: A. mellifera entomoglyceroporin; Aquaporin 1: mammalian aquaporin; AQPcic: C. viridis aquaporin; AQP4: A. aegypti aquaporin. Amino acid residues identical to those in Am_Eglp 1 are shaded. NPA motifs are highlighted in a box. C: cysteine residues close to second NPA motif. B: Hydrophobicity profile of Am_Eglp 1. Numbers 1 through 6 are hydrophobic transmembrane domains. Arrow: NPA motifs. Arrowhead: cysteine position upstream to second NPA motif.
Fig 3. Functional characterization of Am_Eglp 1 via transient expression in Xenopus oocytes.A: Western Blot analysis of lysed oocytes, using anti myc-tag antibody. M: molecular weight. 1: Am_Eglp 1 cRNA injected oocytes. 2: water injected oocytes; 3: uninjected oocytes. Arrow: positive reaction of myc-tagged Am_Eglp 1. B: Permeability coefficient (Pf) analysis of oocytes expressing Am_Eglp 1 subjected to water uptake assay. Am_Eglp 1: oocytes expressing Am_Eglp 1 (n = 14). HgCl2: oocytes expressing Am_Eglp 1 and exposed to mercury prior to water uptake assay (n = 10). H2O: water injected oocytes (n = 6). Ø: non-injected oocytes (n = 9). Values are means ± SD. Means separated by Tukey (p<0.05). Means which share the same letter are not significantly different. C: Water uptake assay. Oocytes expressing Am_Eglp 1 submitted to hyposmotic schock demonstrated a gradual increase in volume due to water uptake throughout testing time. Arrow: cellular membrane rupture.
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