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Hypothesis/review: The structural basis of sweetness perception of sweet-tasting plant proteins can be deduced from sequence analysis

Journal

PLANT SCIENCE
Volume 181, Issue 4, Pages 347-354

Publisher

ELSEVIER IRELAND LTD
DOI: 10.1016/j.plantsci.2011.06.009

Keywords

Sweetness receptor; Sequence analysis; Protein homology; Structure-function; Brazzein; Thaumatin

Funding

  1. Belgian Fund for Scientific Research (FNRS-FRS)
  2. IN-Wallonie-Bruxelles International (Belgium)

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Human perception of sweetness, behind the felt pleasure, is thought to play a role as an indicator of energy density of foods. For humans, only a small number of plant proteins taste sweet. As non-caloric sweeteners, these plant proteins have attracted attention as candidates for the control of obesity, oral health and diabetic management. Significant advances have been made in the characterization of the sweet-tasting plant proteins, as well as their binding interactions with the appropriate receptors. The elucidation of sweet-taste receptor gene sequences represents an important step towards the understanding of sweet taste perception. However, many questions on the molecular basis of sweet-taste elicitation by plant proteins remain unanswered. In particular, why homologues of these proteins do not elicit similar responses? This question is discussed in this report, on the basis of available sequences and structures of sweet-tasting proteins, as well as of sweetness-sensing receptors. A simple procedure based on sequence comparisons between sweet-tasting protein and its homologous counterparts was proposed to identify critical residues for sweetness elicitation. The open question on the physiological function of sweet-tasting plant proteins is also considered. In particular, this review leads us to suggest that sweet-tasting proteins may interact with taste receptor in a serendipity manner. (C) 2011 Elsevier Ireland Ltd. All rights reserved.

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