Characterization of immunoaffinity purified peptidoglycan-associated lipoprotein of Actinobacillus actinomycetemcomitans



: Ihalin R, Karched M, Eneslatt K, Asikainen S

Publisher: ELSEVIER SCIENCE BV

: 2006

: JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES

: J CHROMATOGR B

: 831

: 1-2

: 116

: 125

: 10

: 1570-0232

DOI: https://doi.org/10.1016/j.jchromb.2005.11.052(external)

: https://www.sciencedirect.com/science/article/pii/S1570023205009062?via=ihub(external)


Peptidoglycan-associated lipoprotein (PAL) is a highly conserved structural outer membrane protein among Gram-negative bacteria. In some species, it is proinflammatory and released extracellularly. We purified a newly identified PAL (AaPAL) of a periodontal pathogen Actinobacillus actinomycetemcomitans by using AaPAL antipeptide antibodies coupled to immunoaffinity chromatography column. No protein impurities originating in A. actinomycetemcomitans were found in the final product. Sera from patients infected by A. actinomycetenicomitans recognized the purified AaPAL. The present purification method seems to be suitable for isolation of AaPAL and probably PALs of other bacterial species, and applicable in studies investigating proinflammatory mechanisms of A. actinomyceteincomitans. (c) 2005 Elsevier B.V. All rights reserved.



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