TY - JOUR
T1 - Further evidence that mechanisms of host/symbiont integration are dissimilar in the maternal versus embryonic Acyrthosiphon pisum bacteriome
AU - Banfill, Celeste R.
AU - Wilson, Alex C.C.
AU - Lu, Hsiao ling
N1 - Funding Information:
This work was supported by National Science Foundation Awards IOS-1121847 and IOS-1354154 to ACCW and by Ministry of Science and Technology Awards MOST 108-2313-B-150-001-MY3 to HLL. Acknowledgements
Funding Information:
The authors thank James Baker of the Confocal Microscopy Core Facility in the Department of Biology at the University of Miami. They would also like to thank Chun-che Chang for the provision of the ApVAS1 antibody. This work benefited from discussions with Dinah Hales, who assisted in identifying the corpora cardiaca, and Damian Hernandez who provided feedback on an early draft of the manuscript. This work was supported by National Science Foundation Awards IOS-1121847 and IOS-1354154 to ACCW, and by Ministry of Science and Technology Award MOST 108-2313-B-150-001-MY3 to HLL.
PY - 2020/12
Y1 - 2020/12
N2 - Background: Host/symbiont integration is a signature of evolutionarily ancient, obligate endosymbioses. However, little is known about the cellular and developmental mechanisms of host/symbiont integration at the molecular level. Many insects possess obligate bacterial endosymbionts that provide essential nutrients. To advance understanding of the developmental and metabolic integration of hosts and endosymbionts, we track the localization of a non-essential amino acid transporter, ApNEAAT1, across asexual embryogenesis in the aphid, Acyrthosiphon pisum. Previous work in adult bacteriomes revealed that ApNEAAT1 functions to exchange non-essential amino acids at the A. pisum/Buchnera aphidicola symbiotic interface. Driven by amino acid concentration gradients, ApNEAAT1 moves proline, serine, and alanine from A. pisum to Buchnera and cysteine from Buchnera to A. pisum. Here, we test the hypothesis that ApNEAAT1 is localized to the symbiotic interface during asexual embryogenesis. Results: During A. pisum asexual embryogenesis, ApNEAAT1 does not localize to the symbiotic interface. We observed ApNEAAT1 localization to the maternal follicular epithelium, the germline, and, in late-stage embryos, to anterior neural structures and insect immune cells (hemocytes). We predict that ApNEAAT1 provisions non-essential amino acids to developing oocytes and embryos, as well as to the brain and related neural structures. Additionally, ApNEAAT1 may perform roles related to host immunity. Conclusions: Our work provides further evidence that the embryonic and adult bacteriomes of asexual A. pisum are not equivalent. Future research is needed to elucidate the developmental time point at which the bacteriome reaches maturity.
AB - Background: Host/symbiont integration is a signature of evolutionarily ancient, obligate endosymbioses. However, little is known about the cellular and developmental mechanisms of host/symbiont integration at the molecular level. Many insects possess obligate bacterial endosymbionts that provide essential nutrients. To advance understanding of the developmental and metabolic integration of hosts and endosymbionts, we track the localization of a non-essential amino acid transporter, ApNEAAT1, across asexual embryogenesis in the aphid, Acyrthosiphon pisum. Previous work in adult bacteriomes revealed that ApNEAAT1 functions to exchange non-essential amino acids at the A. pisum/Buchnera aphidicola symbiotic interface. Driven by amino acid concentration gradients, ApNEAAT1 moves proline, serine, and alanine from A. pisum to Buchnera and cysteine from Buchnera to A. pisum. Here, we test the hypothesis that ApNEAAT1 is localized to the symbiotic interface during asexual embryogenesis. Results: During A. pisum asexual embryogenesis, ApNEAAT1 does not localize to the symbiotic interface. We observed ApNEAAT1 localization to the maternal follicular epithelium, the germline, and, in late-stage embryos, to anterior neural structures and insect immune cells (hemocytes). We predict that ApNEAAT1 provisions non-essential amino acids to developing oocytes and embryos, as well as to the brain and related neural structures. Additionally, ApNEAAT1 may perform roles related to host immunity. Conclusions: Our work provides further evidence that the embryonic and adult bacteriomes of asexual A. pisum are not equivalent. Future research is needed to elucidate the developmental time point at which the bacteriome reaches maturity.
KW - Amino acid transporter
KW - Bacteriome
KW - Coevolution
KW - Endosymbiosis
KW - Host/symbiont developmental integration
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U2 - 10.1186/s13227-020-00168-5
DO - 10.1186/s13227-020-00168-5
M3 - Article
AN - SCOPUS:85095690373
VL - 11
JO - EvoDevo
JF - EvoDevo
SN - 2041-9139
IS - 1
M1 - 23
ER -