Page 45
J u l y 2 3 - 2 4 , 2 0 1 8 | R o m e , I t a l y
Note:
allied
academies
Joint Event on
Cardiology Congress 2018 & Microbe Infection 2018
Biomedical Research
|
ISSN: 0976-1683
|
Volume 29
2
nd
World Congress on
CARDIOLOGY
MICROBIOLOGY AND MICROBIAL INFECTION
&
39
th
Annual Congress on
Biomed Res 2018, Volume 29 | DOI: 10.4066/biomedicalresearch-C1-003
FLAGELLAR ASSEMBLY IN
SALMONELLA FLHA
DELETED STRAIN AND ITS
ROLE IN BIOFILM FORMATION
Iram Liaqat
1
and
Shahid Khan
1,2
1
GC University, Pakistan
2
LUMS-School of Science and Engineering, Pakistan
B
iofilms formation is a major hazardous problem from both clinical and environmental perspective. Flagellum-mediated
motility is important for biofilm formation by several gram-negative bacteria. More than 50 genes are involved in flagellar
biosynthesis and function in
Salmonella typhimurium
. The flagella basal body is a representative of type III protein secretion
systems; used by several gram-negative bacterial pathogens to colonize foreign tissues and substrates. The mechanism of
flagellar assembly was analyzed in
S.typhimurium
, using bioinformatics analysis to identify conserved structural elements. In this
study, Flil a flagellar protein that is needed for flagellar assembly and may be involved in a specialized protein export pathway was
cloned and overexpressed.
FlhA
deleted mutant
Salmonella
strain SJW1616 was used to transform
FliI
overproducing plasmid by
electroporation. Using vital dyes (Alexaflour 488), visualization of motility was observed in wild type, SJW1616 (Δ
flhA
) and
FlhA
transductant strain which was further assessed by biofilm formation ability. Swimming, swarmingmotility along with significantly
reduced biofilm formation was observed in SJW1616 (Δ
flhA
) compared to wild type and
FlhA
transductant strains. This study
will extend initial evidence that
FliI
plays important role in flagellar export system and flagellum-mediated rotation is critical for
swimming, swarming motility and biofilm formation. The flagellar basal body is a particularly convenient drug target, since the
architecture of most its components has been determined near atomic resolution and it is an ancient evolutionarily conserved
macromolecular assembly. The knowledge gained will also have implications for elucidation of the mechanistic design principles
underlying protein secretion complexes.
iramliaq@hotmail.com