Crystal and Solution Studies of the “Plus-C” Odorant-binding Protein 48 from Anopheles gambiae

Tsitsanou, Katerina E.; Drakou, C.E.; Thireou, Trias; Gruber, Anna; Kythreoti, Georgia; Azem, Abdussalam; Fessas, Dimitrios; Eliopoulos, Elias; Iatrou, Kostas; Zographos, S.E.

doi:10.1074/jbc.m113.505289

Cited by 36 publications

(28 citation statements)

References 54 publications

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“…2). The OBP Cplus proteins are known to form domain-swapped dimers, using their N-terminal and C-terminal extensions (Tsitsanou et al, 2013). The homology models for OBPL2 did not find a dimer interface, but the question of the oligomeric form of OBPL2 will be examined in future studies.…”

Section: Obp-like Proteinsmentioning

confidence: 96%

The chemosensory appendage proteome of Amblyomma americanum (Acari: Ixodidae) reveals putative odorant‐binding and other chemoreception‐related proteins

et al. 2016

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Proteomic analyses were done on 2 chemosensory appendages of the lone star tick, Amblyomma americanum. Proteins in the fore tarsi, which contain the olfactory Haller's organ, and in the palps, that include gustatory sensilla, were compared with proteins in the third tarsi. Also, male and female ticks were compared. Proteins were identified by sequence similarity to known proteins, and by 3-dimensional homology modeling. Proteomic data were also compared with organ-specific transcriptomes from the tick Rhipicephalus microplus. The fore tarsi express a lipocalin not found in the third tarsi or palps. The fore tarsi and palps abundantly express 2 proteins, which are similar to insect odorant-binding proteins (OBPs). Compared with insect OBPs, the tick OBP-like sequences lacked the cysteine absent in C-minus OBPs, and 1 tick OBP-like sequence had additional cysteines that were similar to C-plus OBPs. Four proteins similar to the antibiotic protein microplusin were found: 2 exclusively expressed in the fore tarsi and 1 exclusively expressed in the palps. These proteins lack the microplusin copper-binding site, but they are modeled to have a significant internal cavity, potentially a ligand-binding site. Proteins similar to the dust mite allergens Der p7 and Der f 7 were found differentially expressed in female fore tarsi. A protein exclusively expressed in the fore tarsi has similarities to Neto, which is known to be involved in clustering of ionotropic glutamate receptors. These results constitute the first report of OBP-like protein sequences in ticks and point to several research avenues on tick chemosensory reception.

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Section: Obp-like Proteinsmentioning

confidence: 96%

The chemosensory appendage proteome of Amblyomma americanum (Acari: Ixodidae) reveals putative odorant‐binding and other chemoreception‐related proteins

et al. 2016

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“…The reversibility results of the PEGylated conjugates clearly indicate that a thermodynamic analysis of the denaturation mechanism is allowed [33]. Accordingly, thermodynamic models [36,37] were applied in order to describe the thermal denaturation of the PEGylated conjugates. A single step model native-to-denatured state was sufficient to obtain a good fit for the two protein-polymer conjugates.…”

Section: Thermodynamic Analysismentioning

confidence: 99%

Thermodynamic stability of myoglobin-poly(ethylene glycol) bioconjugates: A calorimetric study

et al. 2019

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PEGylated proteins are widely used for therapeutic applications, therefore a fundamental understanding of the conjugates' structure and their behaviour in solution is essential to promote new developments in this field. In the present work, myoglobin-poly(ethylene glycol) conjugates were synthesized and studied by using differential scanning calorimetry and UV-visible spectroscopy to obtain information on the bioconjugates' thermodynamic stability, also focusing on the PEG's role on the solvent-protein surface interaction. The overall results of this study indicated a thermal destabilization of the proteins that follows the extent of the bioconjugation without, however, compromising the native structure which remains functional. Moreover, the myoglobin PEGylation prevented the post-denaturation aggregation phenomena and enhanced the protein thermal reversibility. The thermodynamic interpretation of the data indicated that the bioconjugation influences the solvent-exposed protein surface difference between native and denatured state, contributing to the interpretation of the overall protein modification and functionality.

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“…Natural swapping generates dimers that can have physiological advantages over their constitutive monomers (Cafaro et al, 1995; Di Donato et al, 1995; Gotte et al, 2012; Josephson et al, 2001; Liu and Eisenberg, 2002; Tsitsanou et al, 2013), as well as polymers that can contribute to pathogenic states (Bennett et al, 2006; Rousseau et al, 2012; van der Wel, 2012). Engineered swapping has the potential to create self-assembling materials that retain and integrate the activities of the parent proteins or encode for emergent functions.…”

mentioning

confidence: 99%

Engineered Domain Swapping as an On/Off Switch for Protein Function

Karchin

Walker-Kopp

et al. 2015

Chemistry & Biology

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Domain swapping occurs when identical proteins exchange segments in reciprocal fashion. Natural swapping mechanisms remain poorly understood and engineered swapping has the potential for creating self-assembling biomaterials that encode for emergent functions. We demonstrate that induced swapping can be used to regulate function of a target protein. Swapping is triggered by inserting a ‘lever’ protein (ubiquitin) into one of four loops of the ribose binding protein (RBP) target. The lever splits the target, forcing RBP to refold in trans to generate swapped oligomers. Identical RBP-ubiquitin fusions form homo-swapped complexes with the ubiquitin domain acting as the hinge. Surprisingly, some pairs of non-identical fusions swap more efficiently with each other than they do with themselves. NMR experiments reveal that the hinge of these hetero-swapped complexes maps to a region of RBP distant from both ubiquitins. This design is expected to be applicable to other proteins to convert them into functional switches.

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Crystal and Solution Studies of the “Plus-C” Odorant-binding Protein 48 from Anopheles gambiae

Cited by 36 publications

References 54 publications

The chemosensory appendage proteome of Amblyomma americanum (Acari: Ixodidae) reveals putative odorant‐binding and other chemoreception‐related proteins

The chemosensory appendage proteome of Amblyomma americanum (Acari: Ixodidae) reveals putative odorant‐binding and other chemoreception‐related proteins

Thermodynamic stability of myoglobin-poly(ethylene glycol) bioconjugates: A calorimetric study

Engineered Domain Swapping as an On/Off Switch for Protein Function

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