Judith Willis

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Judith H. Willis (born 2 January 1935) is an American biologist currently Professor Emeritus at University of Georgia and fellow of the American Association for the Advancement of Science. [1] [2] Her research frequently involved insect cuticular proteins (CPs) as molecular markers of metamorphic stage, precise role CPs play in constructing insects and annotating the CP genes of Anopheles gambiae , the major vector of malaria. [3]

Selected publications

Willis, J.H. 2018  The evolution and metamorphosis of arthropod proteomics and genomics.  Ann. Rev. Entomol.  63:1-13.

Vannini, L. and J.H. Willis  2016.  Immunolocalization of cuticular proteins in Johnston's organ and the corneal lens of Anopheles gambiae.  Arthropod Structure & Develop.  45:519-535.

Ioannidou, Z S., Theodoropoulou, M.C., Papandreou, N.C., Willis, J.H., Hamodrakas, S.J.  2014.  CutProtFam-Pred: Detection and classification of putative structural cuticular proteins from sequence alone, based on profile Hidden Markov Models.  Insect Biochem. Molec. Biol. 52:51-59.

Cornman, R.S., T. Togawa, W.A. Dunn.  N. He, A.C. Emmons, J.H. Willis.  2008.  Annotation and analysis of a large cuticular protein family with the R&R Consensus in Anopheles gambiae.  BMC Genomics 9:22.

Iconomidou, V.A., J.H. Willis and S.J. Hamodrakas.  2005.  Unique features of the structural model of ‘hard’ cuticle proteins: implications for chitin-protein interactions and cross-linking in cuticle.  Insect Biochem. Molec. Biol.  35:553-560.

Dotson, E.M., A.J. Cornel, J.H. Willis and F.H. Collins. 1998.  A family of pupal-specific cuticular protein genes in the mosquito Anopheles gambiae.  Insect. Biochem. Molec. Biol. 28: 459-472.

Willis, J.H.  1986.  The paradigm of stage specific gene sets in insect metamorphosis:  Time for revision!  Arch. Insect Biochem. Physiol. Suppl. 1:47-57.

Related Research Articles

<i>Anopheles</i> Genus of mosquito

Anopheles is a genus of mosquito first described by J. W. Meigen in 1818. Its members are sometimes called nail mosquitoes or marsh mosquitoes. Many are vectors of the Plasmodium parasite of malaria in birds, reptiles, and mammals including humans. Anopheles gambiae is among the best known, as it transmits one of the most dangerous human malaria parasites, Plasmodium falciparum. No other mosquito genus is a vector of human malaria.

<i>Plasmodium berghei</i> Single celled parasite, rodent malaria

Plasmodium berghei is a single-celled parasite causing rodent malaria. It is in the Plasmodium subgenus Vinckeia.

<i>Anopheles gambiae</i> Species of mosquito

The Anopheles gambiae complex consists of at least seven morphologically indistinguishable species of mosquitoes in the genus Anopheles. The complex was recognised in the 1960s and includes the most important vectors of malaria in sub-Saharan Africa, particularly of the most dangerous malaria parasite, Plasmodium falciparum. It is one of the most efficient malaria vectors known. The An. gambiae mosquito additionally transmits Wuchereria bancrofti which causes lymphatic filariasis, a symptom of which is elephantiasis.

Odorant-binding proteins (OBPs) are small soluble proteins secreted by auxiliary cells surrounding olfactory receptor neurons, including the nasal mucus of many vertebrate species and in the sensillar lymph of chemosensory sensilla of insects. OBPs are characterized by a specific protein domain that comprises six α-helices joined by three disulfide bonds. Although the function of the OBPs as a whole is not well established, it is believed that they act as odorant transporters, delivering the odorant molecules to olfactory receptors in the cell membrane of sensory neurons.

Chemosensory proteins (CSPs) are small soluble proteins which mediate olfactory recognition at the periphery of sensory receptors in insects, similarly to odorant-binding proteins. The typical structure of CSPs is made of six or seven α-helical chains of about 110-120 amino acids, including four cysteines that build two small loops, two adjacent disulfide bridges, and a globular "prism-like" functional structure [5]. Three CSP structures have been solved in moths and locusts [5-8].

<span class="mw-page-title-main">RAB3A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-3A is a protein that in humans is encoded by the RAB3A gene. It is involved in calcium-triggered exocytosis in neurons.

<span class="mw-page-title-main">Juvenile-hormone esterase</span>

The enzyme juvenile hormone esterase (EC 3.1.1.59, systematic name methyl-(2E,6E,10R)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate acylhydrolase, JH esterase) catalyzes the hydrolysis of juvenile hormone:

<span class="mw-page-title-main">RAC2</span> Protein-coding gene in the species Homo sapiens

Rac2 is a small signaling G protein, and is a member of the Rac subfamily of the family Rho family of GTPases. It is encoded by the gene RAC2.

<span class="mw-page-title-main">DYRK1A</span> Protein-coding gene in the species Homo sapiens

Dual specificity tyrosine-phosphorylation-regulated kinase 1A is an enzyme that in humans is encoded by the DYRK1A gene. Alternative splicing of this gene generates several transcript variants differing from each other either in the 5' UTR or in the 3' coding region. These variants encode for at least five different isoforms.

<span class="mw-page-title-main">PEX19</span> Protein-coding gene in the species Homo sapiens

Peroxisomal biogenesis factor 19 is a protein that in humans is encoded by the PEX19 gene.

<span class="mw-page-title-main">USP4</span> Protein-coding gene in the species Homo sapiens

Ubiquitin specific protease 4 (USP4) is an enzyme that cleaves ubiquitin from a number of protein substrates. Prior to the standardization of nomenclature USP4 was known as UNP, and was one of the first deubiquitinating enzymes to be identified in mammals. In the mouse and human the USP4 protein is encoded by a gene containing 22 exons.

<span class="mw-page-title-main">60S ribosomal protein L35</span> Protein found in humans

60S ribosomal protein L35 is a protein that in humans is encoded by the RPL35 gene.

<span class="mw-page-title-main">60S ribosomal protein L23a</span> Protein found in humans

60S ribosomal protein L23a is a protein that in humans is encoded by the RPL23A gene.

Bursicon is an insect hormone which mediates tanning in the cuticle of adult flies.

<span class="mw-page-title-main">KRT85</span>

Keratin, type II cuticular Hb5 is a protein that in humans is encoded by the KRT85 gene.

<span class="mw-page-title-main">OrthoDB</span>

OrthoDB presents a catalog of orthologous protein-coding genes across vertebrates, arthropods, fungi, plants, and bacteria. Orthology refers to the last common ancestor of the species under consideration, and thus OrthoDB explicitly delineates orthologs at each major radiation along the species phylogeny. The database of orthologs presents available protein descriptors, together with Gene Ontology and InterPro attributes, which serve to provide general descriptive annotations of the orthologous groups, and facilitate comprehensive orthology database querying. OrthoDB also provides computed evolutionary traits of orthologs, such as gene duplicability and loss profiles, divergence rates, sibling groups, and gene intron-exon architectures.

Thioester containing protein 1, often called TEP1 is a key component of the arthropod innate immune system. TEP1 was first identified as a key immunity gene in 2001 through functional studies on Anopheles gambiae mosquitoes.

<span class="mw-page-title-main">Insect olfaction</span> Function of chemical receptors

Insect olfaction refers to the function of chemical receptors that enable insects to detect and identify volatile compounds for foraging, predator avoidance, finding mating partners and locating oviposition habitats. Thus, it is the most important sensation for insects. Most important insect behaviors must be timed perfectly which is dependent on what they smell and when they smell it. For example, olfaction is essential for locating host plants and hunting prey in many species of insects, such as the moth Deilephila elpenor and the wasp Polybia sericea, respectively.

Juvenile hormone acid O-methyltransferase (JHAMT) is a ~33 kDa enzyme that catalyzes the conversion of inactive precursors of Juvenile hormones (JHs) to active JHs in the final stages of JH biosynthesis in the corpora allata of insects. More specifically, the enzyme catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to the carboxylate group of JH precursors.

Nora J. Besansky is an American molecular biologist. She is the Martin J. Gillen Professor of Biological Sciences at the University of Notre Dame. In 2020, Besansky was elected a Member of the National Academy of Sciences for being an expert in the genomics of malaria vectors.

References

  1. "Entomological society of America".
  2. "University of Georgia Office of Research".
  3. "Judith H. Willis". uga.edu. Retrieved April 26, 2017.