Publish in OALib Journal
APC: Only $99
Interactions between the light-harvesting subunits
and the non-covalently bound photopigments attribute considerably to the
spectral properties of photosynthetic bacteria light-harvesting complexes. In
our previous studies, we have constructed a novel Rhodobacter sphaeroides expression system. In the present study,
we focus on the spectral properties of LH2 when heterologously express LH2 with β-subunit- GFP fusion protein in Rb. sphaeroides. Near infra-red
spectrum of LH2 remained nearly unchanged as measured by spectroscopy.
Fluorescence spectrum suggested that the LH2 with β-subunit-GFP fusion protein complexes still possessed normal
activity in energy transfer. However, photopigments contents were
significantly decreased to a very low level in the LH2
with β-subunit-GFP fusion protein
complexes compared to that of LH2. FT-IR spectra indicated that interactions
between photopigments and LH2 α/β- subunits appeared not to be changed.
It was concluded that the LH2 spectral properties exhibited very similar even
when heterologously expressed LH2 b-subunit
fusion protein in Rb. sphaeroides.
Our present study may supply a new insight into better understand the interactions
between light-harvesting subunits and photopigments and bacterial photosynthesis
and promote the development of the novel Rb.
sphaeroides expression system.
Antibiotic resistant Escherichia coli strains are becoming more common recently. OmpA
is a very important antigen protein of E.
coli, which consists of two separate domains, N-terminal and C-terminal
domain. The N-terminal domain contains eight β- barrel regions that plays important roles in the multifaceted
functions of OmpA. In the present study, we cloned a mutant OmpA gene from a
multi-antibiotic resistant E. coli strain. Sequence analysis indicated that the N-terminal DNA sequence of the
mutant OmpA shared 81.05% homology with the modeled OmpA from E. coli K12 and the N-terminal amino
acid sequence of the mutant OmpA was 81.22% identical to that of the E. coli K12 OmpA. Moreover, several
amino acids located in the β-barrel
region were mutated. The mutant OmpA was expressed in BL21 suggested by
SDS-PAGE. Resistance to environmental stress assay indicated that the
N-terminus mutant OmpA still possessed excellent activities in pH, temperature
and osmotic pressure resistance. Our pre- sent study may supply insights into
better and deeper understand the relationships between OmpA N-terminal
regions and its functions in environmental stress conditions and the mechanisms
on antibiotic resistance of E. coli.
The Seppic Company
developed a new adjuvant Montanide ISA 201
VG, the upgraded version of Montanide ISA 206 VG, which keep the advantage and
added some chemical components on the basis of ISA 206 to improve the cellular
responses. The aim of the study is to compare the efficacy of swine FMD
(foot-and-mouth) vaccine emulsified with oil adjuvant of ISA 201 or ISA 206
respectively. The pigs were vaccinated with FMD vaccine emulsified with
inactive FMD type O antigen and adjuvant ISA 201 or ISA 206 respectively,
according to 2.0 ml (1/1 dose), 0.67 ml (1/3
dose), 0.22 ml (1/9 dose) to calculate their PD50. The
sera were collected from the vaccination of the day 0, 3, 7, 14, 21, 28 and the
ELISA FMD type O antibody were detected. Furthermore, the PD50 were calculated
after the pigs were challenged with virulent
FMDV type O on 28 days post vaccination. The ELISA antibody titers of
201vaccine were significantly
higher than that of 206 (except the third time). The fifty percent of
protection dose (PD50) of 201 vaccine (PD50 = 15.59) was higher than that of 206 vaccine
(PD50 = 10.05). The above data showed that the
efficacy of the FMD vaccine emulsified with ISA 201 was better than which with