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The BPI-like/PLUNC family proteins in cattle
Thomas T Wheeler1, Brendan J Haigh, Marita K Broadhurst
1Agri-Foods and Health Section, AgResearch, Ruakura Research Centre, Hamilton, New Zealand. tom.wheeler@agresearch.co.nz
Biochemical Society Transactions
|July 27, 2011
Summary
Bovine salivary protein 30 kDa (BSP30) belongs to the bactericidal/permeability increasing protein (BPI)-like family. This review explores BSP30
Area of Science:
- Biochemistry
- Genomics
- Immunology
Background:
- Bactericidal/permeability increasing protein (BPI)-like proteins are found in mammals but poorly characterized outside humans and mice.
- Cattle BPI-like proteins offer insights into ruminant physiology and evolution.
- The BPI-like locus in cattle includes multiple bovine salivary protein 30 kDa (BSP30) genes derived from an ancestral gene shared with parotid secretory protein (PSP).
Purpose of the Study:
- To review the current understanding of BPI-like proteins in cattle.
- To investigate the evolution, expression, and function of BSP30 proteins.
- To explore the role of BSP30 in host defense and ruminant digestion.
Main Methods:
- Literature review of existing studies on cattle BPI-like proteins.
- Analysis of gene duplication events and evolutionary relationships.
- Summary of expression patterns across bovine tissues.
- Compilation of functional data including antimicrobial and binding activities.
Main Results:
- Multiple BSP30 genes arose from duplications of an ancestral gene.
- BSP30 proteins are abundant in cattle saliva and salivary tissues.
- Expression is independently regulated at sites of high pathogen exposure.
- BSP30 exhibits antimicrobial, lipopolysaccharide-binding, and bacterial aggregation activities.
Conclusions:
- BSP30 proteins play a significant role in bovine host defense.
- Their functions may be linked to the unique digestive physiology of ruminants.
- Further research on BPI-like proteins in cattle can illuminate host-microbe interactions in ruminants.
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