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Biophysical analysis of anopheles gambiae leucine-rich repeat proteins APL1A1, APL1B [corrected] and APL1C and their interaction with LRIM1.

<div class='caption-title'>Schematic diagram of the LRIM1 and APL1 proteins.</div>
<div class='caption-title'>SAXS modeling of TEP1*R1, LRIM1-LRR, APL1C-LRR and LRIM1/APL1C.</div>
<div class='caption-title'>Solution State of LRIM1 and APL1A—C LRR domains.</div>
Williams M, Summers BJ, Baxter RH
OpenAccess logo PLoS One 10 e0118911 (2015)
Cited: 11 times
EuropePMC logo PMID: 25775123

Abstract

Natural infection of Anopheles gambiae by malaria-causing Plasmodium parasites is significantly influenced by the APL1 genetic locus. The locus contains three closely related leucine-rich repeat (LRR) genes, APL1A, APL1B and APL1C. Multiple studies have reported the participation of APL1A-C in the immune response of A. gambiae to invasion by both rodent and human Plasmodium isolates. APL1C forms a heterodimer with the related LRR protein LRIM1 via a C-terminal coiled-coil domain that is also present in APL1A and APL1B. The LRIM1/APL1C heterodimer protects A. gambiae from infection by binding the complement-like protein TEP1 to form a stable and active immune complex. Here we report solution x-ray scatting data for the LRIM1/APL1C heterodimer, the oligomeric state of LRIM1/APL1 LRR domains in solution and the crystal structure of the APL1B LRR domain. The LRIM1/APL1C heterodimeric complex has a flexible and extended structure in solution. In contrast to the APL1A, APL1C and LRIM1 LRR domains, the APL1B LRR domain is a homodimer. The crystal structure of APL1B-LRR shows that the homodimer is formed by an N-terminal helix that complements for the absence of an N-terminal capping motif in APL1B, which is a unique distinction within the LRIM1/APL1 protein family. Full-length APL1A1 and APL1B form a stable complex with LRIM1. These results support a model in which APL1A1, APL1B and APL1C can all form an extended, flexible heterodimer with LRIM1, providing a repertoire of functional innate immune complexes to protect A. gambiae from a diverse array of pathogens.

Articles - 4xgo mentioned but not cited (1)

  1. Biophysical analysis of anopheles gambiae leucine-rich repeat proteins APL1A1, APL1B [corrected] and APL1C and their interaction with LRIM1. Williams M, Summers BJ, Baxter RH. PLoS ONE 10 e0118911 (2015)


Reviews citing this publication (2)

  1. Mosquito gut antiparasitic and antiviral immunity. Saraiva RG, Kang S, Simões ML, Angleró-Rodríguez YI, Dimopoulos G. Dev. Comp. Immunol. 64 53-64 (2016)
  2. In a Class of Their Own - RXFP1 and RXFP2 are Unique Members of the LGR Family. Petrie EJ, Lagaida S, Sethi A, Bathgate RA, Gooley PR. Front Endocrinol (Lausanne) 6 137 (2015)

Articles citing this publication (8)

  1. A key malaria metabolite modulates vector blood seeking, feeding, and susceptibility to infection. Emami SN, Lindberg BG, Hua S, Hill SR, Mozuraitis R, Lehmann P, Birgersson G, Borg-Karlson AK, Ignell R, Faye I. Science 355 1076-1080 (2017)
  2. An Evolution-Based Screen for Genetic Differentiation between Anopheles Sister Taxa Enriches for Detection of Functional Immune Factors. Mitri C, Bischoff E, Takashima E, Williams M, Eiglmeier K, Pain A, Guelbeogo WM, Gneme A, Brito-Fravallo E, Holm I, Lavazec C, Sagnon N, Baxter RH, Riehle MM, Vernick KD. PLoS Pathog. 11 e1005306 (2015)
  3. Bombyx mori and Aedes aegypti form multi-functional immune complexes that integrate pattern recognition, melanization, coagulants, and hemocyte recruitment. Phillips DR, Clark KD. PLoS ONE 12 e0171447 (2017)
  4. Stimulation of a protease targeting the LRIM1/APL1C complex reveals specificity in complement-like pathway activation in Anopheles gambiae. Reyes Ruiz VM, Sousa GL, Sneed SD, Farrant KV, Christophides GK, Povelones M. PLoS ONE 14 e0214753 (2019)
  5. Transcriptional Profile of Aedes aegypti Leucine-Rich Repeat Proteins in Response to Zika and Chikungunya Viruses. Zhao L, Alto BW, Shin D. Int J Mol Sci 20 (2019)
  6. Anopheles gambiae TEP1 forms a complex with the coiled-coil domain of LRIM1/APL1C following a conformational change in the thioester domain. Williams M, Contet A, Hou CD, Levashina EA, Baxter RHG. PLoS ONE 14 e0218203 (2019)
  7. Published Erratum Correction: Biophysical Analysis of Anopheles gambiae Leucine-Rich Repeat Proteins APL1A1, APL1B and APL1C and Their Interaction with LRIM1. PLOS ONE Staff. PLoS ONE 10 e0126901 (2015)
  8. Functional Constraints on Insect Immune System Components Govern Their Evolutionary Trajectories. Ruzzante L, Feron R, Reijnders MJMF, Thiébaut A, Waterhouse RM. Mol Biol Evol 39 msab352 (2022)


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