Affiliation:
1. Department of Food Science
2. Centre for Advanced Food Studies, The Royal Veterinary and Agricultural University, Frederiksberg
3. Applied Biotechnology, Chr. Hansen A/S, Hørsholm, Denmark
Abstract
ABSTRACT
The aim of this work was to identify genes in
Lactococcus lactis
subsp.
lactis
IL1403 and
Lactococcus lactis
subsp.
cremoris
Wg2 important for adsorption of the 936-species phages bIL170 and φ645, respectively. Random insertional mutagenesis of the two
L. lactis
strains was carried out with the vector pGh9:IS
S1
, and integrants that were resistant to phage infection and showed reduced phage adsorption were selected. In
L. lactis
IL1403 integration was obtained in the
ycaG
and
rgpE
genes, whereas in
L. lactis
Wg2 integration was obtained in two genes homologous to
ycbC
and
ycbB
of
L. lactis
IL1403.
rgpE
and
ycbB
encode putative glycosyltransferases, whereas
ycaG
and
ycbC
encode putative membrane-spanning proteins with unknown functions. Interestingly,
ycaG
,
rgpE
,
ycbC
, and
ycbB
are all part of the same operon in
L. lactis
IL1403. This operon is probably involved in biosynthesis and transport of cell wall polysaccharides (WPS). Binding and infection studies showed that φ645 binds to and infects
L. lactis
Wg2,
L. lactis
IL1403, and
L. lactis
IL1403 strains with pGh9:IS
S1
integration in
ycaG
and
rgpE
, whereas bIL170 binds to and infects only
L. lactis
IL1403 and cannot infect Wg2. These results indicate that φ645 binds to a WPS structure present in both
L. lactis
IL1403 and
L. lactis
Wg2, whereas bIL170 binds to another WPS structure not present in
L. lactis
Wg2. Binding of bIL170 and φ645 to different WPS structures was supported by alignment of the receptor-binding proteins of bIL170 and φ645 that showed no homology in the C-terminal part.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
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