LBP/BPI proteins and their relatives: conservation over evolution and roles in mutualism

LBP [LPS (lipopolysaccharide)-binding protein] and BPI (bactericidal/permeability-increasing protein) are components of the immune system that have been principally studied in mammals for their involvement in defence against bacterial pathogens. These proteins share a basic architecture and residues...

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Published inBiochemical Society transactions Vol. 39; no. 4; p. 1039
Main Authors Krasity, Benjamin C, Troll, Joshua V, Weiss, Jerrold P, McFall-Ngai, Margaret J
Format Journal Article
LanguageEnglish
Published England 01.08.2011
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Abstract LBP [LPS (lipopolysaccharide)-binding protein] and BPI (bactericidal/permeability-increasing protein) are components of the immune system that have been principally studied in mammals for their involvement in defence against bacterial pathogens. These proteins share a basic architecture and residues involved in LPS binding. Putative orthologues, i.e. proteins encoded by similar genes that diverged from a common ancestor, have been found in a number of non-mammalian vertebrate species and several non-vertebrates. Similar to other aspects of immunity, such as the activity of Toll-like receptors and NOD (nucleotide-binding oligomerization domain) proteins, analysis of the conservation of LBPs and BPIs in the invertebrates promises to provide insight into features essential to the form and function of these molecules. This review considers state-of-the-art knowledge in the diversity of the LBP/BPI proteins across the eukaryotes and also considers their role in mutualistic symbioses. Recent studies of the LBPs and BPIs in an invertebrate model of beneficial associations, the Hawaiian bobtail squid Euprymna scolopes' alliance with the marine luminous bacterium Vibrio fischeri, are discussed as an example of the use of non-vertebrate models for the study of LBPs and BPIs.
AbstractList LBP [LPS (lipopolysaccharide)-binding protein] and BPI (bactericidal/permeability-increasing protein) are components of the immune system that have been principally studied in mammals for their involvement in defence against bacterial pathogens. These proteins share a basic architecture and residues involved in LPS binding. Putative orthologues, i.e. proteins encoded by similar genes that diverged from a common ancestor, have been found in a number of non-mammalian vertebrate species and several non-vertebrates. Similar to other aspects of immunity, such as the activity of Toll-like receptors and NOD (nucleotide-binding oligomerization domain) proteins, analysis of the conservation of LBPs and BPIs in the invertebrates promises to provide insight into features essential to the form and function of these molecules. This review considers state-of-the-art knowledge in the diversity of the LBP/BPI proteins across the eukaryotes and also considers their role in mutualistic symbioses. Recent studies of the LBPs and BPIs in an invertebrate model of beneficial associations, the Hawaiian bobtail squid Euprymna scolopes' alliance with the marine luminous bacterium Vibrio fischeri, are discussed as an example of the use of non-vertebrate models for the study of LBPs and BPIs.
Author Krasity, Benjamin C
Weiss, Jerrold P
Troll, Joshua V
McFall-Ngai, Margaret J
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Snippet LBP [LPS (lipopolysaccharide)-binding protein] and BPI (bactericidal/permeability-increasing protein) are components of the immune system that have been...
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StartPage 1039
SubjectTerms Acute-Phase Proteins - genetics
Acute-Phase Proteins - metabolism
Amino Acid Sequence
Animals
Antimicrobial Cationic Peptides - genetics
Antimicrobial Cationic Peptides - metabolism
Blood Proteins - genetics
Blood Proteins - metabolism
Carrier Proteins - genetics
Carrier Proteins - metabolism
Conserved Sequence
Evolution, Molecular
Humans
Lipid Metabolism
Membrane Glycoproteins - genetics
Membrane Glycoproteins - metabolism
Models, Biological
Protein Binding
Sequence Homology, Amino Acid
Symbiosis - physiology
Title LBP/BPI proteins and their relatives: conservation over evolution and roles in mutualism
URI https://www.ncbi.nlm.nih.gov/pubmed/21787344
Volume 39
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