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{| cellpadding="10" style="background:#003366; width:800px;"
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<font size="6" color="#ffffff">Laboratory of Immunogenomics</font><BR>&nbsp;<BR>
[[Kafatos:Kafatos/Christophides Lab|Kafatos/Christophides Lab]]
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{{Kafatos/Christophides Lab}}
 
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<font size="5">'''Michael Povelones'''</font size>
<TR>
</div>&nbsp;<BR>
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<font size="6" color="#555555">'''Michael Povelones'''</font>
<div style="padding: 15px; color: #ffffff; background-color: #3674C2; width: 250px">
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<font size="3" color="#ffffff">Division of Cell & Molecular Biology<br>[[image:Kafatos-white-mosquito.png|right]]
</TR>
Imperial College<br>
<TR>
<TD>
<font size="3" color="#333333" class="mainfont">Division of Cell & Molecular Biology<br>
Imperial College London<br>
South Kensington Campus<br>
South Kensington Campus<br>
SAF Building<br>
SAF Building, 6th Floor<br>
London, SW7 2AZ<br>
London, SW7 2AZ<br>
United Kingdom<br>
United Kingdom<br>
[[Image:Kafatos-pove-email.png]]
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<TD>
[[Kafatos-pove-edu-prev-research|Education & Previous Research]]
</TD>
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</TABLE>
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|}
 
----
__NOTOC__
__NOTOC__
 
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===Education===


===Current Research Interests===
<font class="mainfont">I am a postdoctoral fellow in the [[kafatos:Kafatos/Christophides Lab|Kafatos/Christophides lab]] at [http://www.imperial.ac.uk/ Imperial College London]. My research focuses on how the innate immune system of the mosquito recognizes and eliminates malaria parasites. Though it is not widely known, mosquitoes are amazing parasite killers. In fact, the vast majority of the parasites ingested when a mosquito bites a malarious person are attacked and eliminated before they can mount an infection. It is the few parasites that survive (one is enough), that are ultimately responsible for disease transmission. 


<font size="3">
* BA in Chemistry, [http://www.columbia.edu Columbia University], New York, NY, USA
* PhD in Developmental Biology, [http://www.stanford.edu Stanford University], Stanford, CA, USA
* Biology of Parasitism 2005, [http://www.mbl.edu MBL], Woods Hole, MA


</font>
The mosquito has multiple lines of defense, but the most potent is found in its blood (hemolymph). Parasites contact the mosquito blood when they cross the gut cells as they try to escape the harsh digestive conditions of the gut lumen. Two Leucine-rich repeat (LRR) containing proteins, LRIM1 and APL1C, orchestrate the mosquito immune defense. We recently found that these proteins circulate in the mosquito hemolymph in a disulfide-bonded multimeric complex <cite>Pove-Science-2009</cite>. If either LRIM1 or APL1C is knocked-down by RNAi the complex is lost from the hemolymph. Before parasites are killed, the complement-like protein TEP1 is localized on their surface, marking them for destruction. The LRIM1/APL1C complex interacts with the complement-like protein TEP1 and is required for TEP1 localization to parasites during midgut invasion. When the LRIM1/APL1C complex is knocked-down by RNAi, TEP1 fails to localize and the invading parasites are not killed. This immune pathway leading to parasite killing can be an important cause of natural refractoriness in non-vector mosquitoes <cite>Habtewold-PLoS_Pathogens-2008</cite>. Fully understanding the mechanism of parasite killing and why some parasites manage to escape may open the door to novel control strategies.
|}




{|cellspacing="5" cellpadding="10" style="background:#3674C2; width: 800px;"
We found that LRIM1 and APL1C are defining members of a protein family, named LRIMs (pronounced L-rims) <cite>Pove-Science-2009</cite>. Bioinformatic searches using specific features shared between LRIM1 and APL1C has uncovered approximately 20 family members falling into four distinct sub-families in Anopheles gamibae, Aedes aegypti and Culex quinquefasciatus but none in any other organisms. Given the central role of LRR proteins in host defense in plants and animals, we are currently investigating the hypothesis that the repertoire of LRIMs may help the mosquito neutralize diverse pathogens, including the agents of human and animal diseases that they transmit.</font>
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===Current Research Interests===
<font size="3">I am a postdoctoral fellow in the [[kafatos:Kafatos/Christophides Lab|Kafatos/Christophides Lab]] at [http://www.imperial.ac.uk/ Imperial College], London. Science is cool.</font>


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* [[pmid:19264986 | Povelones M, Waterhouse RM, Kafatos FC, Christophides GK. Leucine-Rich Repeat Protein Complex Activates Mosquito Complement in Defense Against Plasmodium Parasites. Science 2009 March 5 (Epub ahead of print)]]
<biblio>
* [[pmid:18497855 |Habtewold T, Povelones M, Blagborough AM, Christophides GK. Transmission Blocking Immunity in the Malaria Non-Vector Mosquito ''Anopheles quadriannulatus'' Species A. PLoS Pathog. 2008 May 23;4(5).]]
#Pove-Science-2009 pmid=19264986
#Habtewold-PLoS_Pathogens-2008 pmid=18497855
</biblio>
</div>
</div>


|}
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===Previous Research===
<font size="3">I received my doctoral degree at [http://www.stanford.edu Stanford University] in the laboratory of [http://www.stanford.edu/~rnusse/ Roel Nusse]. The focus of my research was understanding how the ''frizzled (fz)'' receptor in ''Drosophila'' functions in planar cell polarization (PCP) and Wnt-mediated cell fate specification. ''fz'' controls two different signal transduction pathways for each of these distinct developmental outcomes. How does a single receptor function in two signaling pathways? This work revealed that even though cell fate signaling requires a Wnt ligand, ''fz'' is not activated by any of the 7 ''Drosophila'' Wnt genes for its PCP function. Instead, ''fz'' has an intrinsic ability to control components of the PCP pathway and that it associates with pathway specific Wnt co-receptor for cell fate signaling. In addition, a structure-function analysis of ''fz'' suggested that, in addition to the Wnt binding site located in the extracellular cysteine-rich domain, there is a second Wnt-binding site within the transmembrane portion of the receptor.</font>
[[Image:Kafatos-pove-fz.png|right|220px]]
<div style="padding: 10px; color:#000000; background-color: #DBEAFF; width: 500px">
* [[pmid:16163385|Povelones M and Nusse R. The role of the cysteine-rich domain of Frizzled in Wingless-Armadillo signaling. EMBO J 2005 Oct 5; 24(19) 3493-503.]]
* [[pmid:16085697|Povelones M, Howes R, Fish M, and Nusse R. Genetic evidence that Drosophila frizzled controls planar cell polarity and Armadillo signaling by a common mechanism. Genetics 2005 Dec; 171(4) 1643-54.]]
* [[pmid:12415278|Povelones M and Nusse R. Wnt signalling sees spots. Nat Cell Biol 2002 Nov; 4(11) E249-50.]]
* [[pmid: 18555784|Chen WS, Antic D, Matis M, Logan CY, Povelones M, Anderson GA, Nusse R, Axelrod JD. Asymmetric homotypic interactions of the atypical cadherin flamingo mediate intercellular polarity signaling. Cell. 2008 Jun 13;133(6):1093-105.]]
</div>
<font size="3">I worked in the laboratory of [http://www.cumc.columbia.edu/dept/gsas/anatomy/Faculty/Ambron/index.html Richard Ambron] as an undergraduate and research technician at [http://www.columbia.edu Columbia University]. The focus of this research was the identification of intrinsic nerve injury signals. In addition to growth factor and electrophysiological responses, neurons posses axonal proteins with a masked nuclear localization sequence (NLS) that serve as a sensor for injury. These injury signals are activated and rapidly retrogradely transported to the neuronal cell body and into the nucleus following nerve crush injury. In the nucleus they function to initiate the transcriptional program for repair. My research focused on the identification of an NF-&kappa;B-like transcription factor in Aplysia and its function in nerve injury. Nerve regeneration following injury requires transcriptional activation of repair genes. Members NF-&kappa;B family of transcription factors are well-suited to play a role in nerve injury since they contain and masked NLS and are localized to the cytoplasm until activated. This work identified by electrophoretic mobility shift assay an NF-&kappa;B-like activity in axoplasm. Contrary to what was expected, this activity was rapidly inactivated in injured neurons. We hypothesized that in these neurons, NF-&kappa;B functions as a signal of homeostasis and must be inactivated following injury since it regulates genes that are incompatible with repair. </font>
[[Image:kafatos-injured-neuron.png|right]]
<div style="padding: 10px; color:#000000; background-color: #DBEAFF; width: 500px">
* [[pmid:11257614|Sung YJ, Povelones M, and Ambron RT. RISK-1: a novel MAPK homologue in axoplasm that is activated and retrogradely transported after nerve injury. J Neurobiol 2001 Apr; 47(1) 67-79.]]
* [[pmid:11153011|Farr M, Zhu DF, Povelones M, Valcich D, and Ambron RT. Direct interactions between immunocytes and neurons after axotomy in Aplysia. J Neurobiol 2001 Feb 5; 46(2) 89-96.]]
* [[pmid:9185529|Povelones M, Tran K, Thanos D, and Ambron RT. An NF-kappaB-like transcription factor in axoplasm is rapidly inactivated after nerve injury in Aplysia. J Neurosci 1997 Jul 1; 17(13) 4915-20.]]
* [[pmid:8922402|Ambron RT, Zhang XP, Gunstream JD, Povelones M, and Walters ET. Intrinsic injury signals enhance growth, survival, and excitability of Aplysia neurons. J Neurosci 1996 Dec 1; 16(23) 7469-77.]]
</div>
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[[kafatos:pove_new new_page]]

Revision as of 12:20, 31 March 2009

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Laboratory of Immunogenomics
 
Kafatos/Christophides Lab


Michael Povelones

Division of Cell & Molecular Biology
Imperial College London
South Kensington Campus
SAF Building, 6th Floor
London, SW7 2AZ
United Kingdom

Education & Previous Research

Current Research Interests

I am a postdoctoral fellow in the Kafatos/Christophides lab at Imperial College London. My research focuses on how the innate immune system of the mosquito recognizes and eliminates malaria parasites. Though it is not widely known, mosquitoes are amazing parasite killers. In fact, the vast majority of the parasites ingested when a mosquito bites a malarious person are attacked and eliminated before they can mount an infection. It is the few parasites that survive (one is enough), that are ultimately responsible for disease transmission.


The mosquito has multiple lines of defense, but the most potent is found in its blood (hemolymph). Parasites contact the mosquito blood when they cross the gut cells as they try to escape the harsh digestive conditions of the gut lumen. Two Leucine-rich repeat (LRR) containing proteins, LRIM1 and APL1C, orchestrate the mosquito immune defense. We recently found that these proteins circulate in the mosquito hemolymph in a disulfide-bonded multimeric complex [1]. If either LRIM1 or APL1C is knocked-down by RNAi the complex is lost from the hemolymph. Before parasites are killed, the complement-like protein TEP1 is localized on their surface, marking them for destruction. The LRIM1/APL1C complex interacts with the complement-like protein TEP1 and is required for TEP1 localization to parasites during midgut invasion. When the LRIM1/APL1C complex is knocked-down by RNAi, TEP1 fails to localize and the invading parasites are not killed. This immune pathway leading to parasite killing can be an important cause of natural refractoriness in non-vector mosquitoes [2]. Fully understanding the mechanism of parasite killing and why some parasites manage to escape may open the door to novel control strategies.


We found that LRIM1 and APL1C are defining members of a protein family, named LRIMs (pronounced L-rims) [1]. Bioinformatic searches using specific features shared between LRIM1 and APL1C has uncovered approximately 20 family members falling into four distinct sub-families in Anopheles gamibae, Aedes aegypti and Culex quinquefasciatus but none in any other organisms. Given the central role of LRR proteins in host defense in plants and animals, we are currently investigating the hypothesis that the repertoire of LRIMs may help the mosquito neutralize diverse pathogens, including the agents of human and animal diseases that they transmit.


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