Alterations of protein synthesis in the cyanobacterium Synechocystis sp. PCC 6803 after a salt shock

Hagemann, Martin; Wölfel, L.; Krüger, B.

doi:10.1099/00221287-136-7-1393

Cited by 58 publications

(26 citation statements)

References 20 publications

(16 reference statements)

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“…It was a lag phase (3 days Vazquez-Duhalt and Arredondo-Vega 1991). Hagemann et al (1990) showed that immediately after NaCl was added to the medium, total protein synthesis in Synechocystis sp. PCC 6803 was almost completely repressed; repression of the synthesis of some proteins in Anabaena sp.…”

Section: Discussionmentioning

confidence: 99%

Effect of salinity on the biochemical composition of the alga Botryococcus braunii Kütz IPPAS H-252

2010

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The effect of 0.3 and 0.7 M NaCl on biomass yield, total nitrogen content, intracellular lipid content, and fatty acid profile of the lipids of the alga Botryococcus braunii IPPAS H-252 in different phases of the culture cycle was studied. The presence of sodium chloride in the medium inhibited the growth of algal cells for the first 3 days of the experiment, causing a decrease in total nitrogen, enhanced synthesis of triacylglycerols, and considerable changes in the lipid fatty acid profile: decreases in polyenoic acid contents (from 68.34% to 29.38% and 12.8%) and proportions of long-chain saturated acids (from 0.53% to 5.3% and 14.13% of the total fatty acids) at 0.3 M NaCl and 0.7 M NaCl, respectively. In later phases of the culture, at 0.3 M NaCl, the content of polyenoic acids rose to the values characteristic of the active growth phase of this alga. At 0.7 M NaCl, the proportion of polyenoic acids grew less significantly, but biomass concentration and total nitrogen increased, similarly to the experiment with 0.3 M NaCl.

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Section: Discussionmentioning

confidence: 99%

Effect of salinity on the biochemical composition of the alga Botryococcus braunii Kütz IPPAS H-252

2010

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“…They include certain integrins (14,15), receptors for angiogenic growth factors (16), proteases (17)(18)(19), and membrane proteins of unknown functions (20,21). Pericytes of angiogenic vessels express a membrane proteoglycan known as NG2 or high molecular weight melanoma antigen (22,23), and the extracellular matrix of angiogenic vessels contains an alternatively spliced form of fibronectin (24).…”

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confidence: 99%

A fragment of the HMGN2 protein homes to the nuclei of tumor cells and tumor endothelial cells in vivo

Porkka

Laakkonen²,

Hoffman³

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

259

220

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“…The latter anti-id mAb was derived from a mouse immunized with the HMW-MAA-specific idiotypic mAb 763.74 (13). This antigen system was selected for our studies, since anti-id mAb MK2-23 has been found to elicit HMW-MAAspecific antibodies in mice and rabbits (14,15), both of which express orthologs of human HMW-MAA constitutively (16,17). In addition, anti-id mAb MK2-23 was able to induce HMW-MAA-specific humoral responses in patients with melanoma (18,19).…”

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confidence: 99%

Structural Basis of Antigen Mimicry in a Clinically Relevant Melanoma Antigen System

Chang¹,

Hernandez-Guzman

Luo³

et al. 2005

Journal of Biological Chemistry

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Although mimics of human tumor antigens are effective immunogens to overcome host unresponsiveness to the nominal antigen, the structural basis of this mimicry remains poorly defined. Therefore, in this study we have characterized the structural basis of the human high molecular weight-melanoma-associated antigen (HMW-MAA) mimicry by the mouse anti-idiotypic (anti-id) monoclonal antibody (mAb) MK2-23. Using x-ray crystallography, we have characterized the three-dimensional structure of the anti-id mAb MK2-23 Fab and shown that its heavy chain complementarity-determining region (CDR3) (H3) and its light chain CDR1 (L1) are closely associated. These moieties are the source of HMW-MAA mimicry, since they display partial amino acid sequence homology along with a similar structural fold with the HMW-MAA core protein. Furthermore, a 15-residue peptide comprising the H3 loop of anti-id mAb MK2-23 demonstrates HMW-MAA-like in vitro and in vivo reactivity. This peptide in conjunction with the structural data will facilitate the characterization of the effect of the degree of antigen mimicry on the induction of a self-antigen-specific immune response by a mimic.Antigen mimicry has been implicated in the pathogenesis of several pathophysiological conditions such as viral immune evasion (1-3) and autoimmunity (4 -7). In these situations, the structurally similar foreign moieties either interfere with the normal biological functions mediated by their nominal counterparts or elicit unwanted immune responses against the host antigens. The consequences sometimes can be quite detrimental. Nevertheless, in the case of autoimmune responses mediated by molecular mimicry, an intriguing finding is the restriction of the damage to an organ or a tissue. This pattern is distinct from the general immune hyper-responsiveness caused by suppression of the regulatory arm of the immune system, such as cytotoxic T lymphocyte antigen-4 (CTLA-4) blockade (8, 9).The potential ability of molecular mimicry to target a specific host antigen has provided the rationale for its use to elicit and/or enhance an immune response against human tumor antigens that are mostly non-mutated self-antigens and therefore poorly or non-immunogenic in patients (for review, see Refs. 10 and 11). Various types of tumor antigen mimics have been identified (for review, see Ref. 11). Among them the most extensively utilized is represented by antiidiotypic (anti-id) 4 monoclonal antibodies (mAb), which have been developed in several human tumor antigen systems (for review, see Refs. 10 and 11). Anti-id mAb markedly differ in their immunogenicity as measured by their ability to elicit a humoral immune response to the corresponding self-tumor antigen. The cause of this variability is not known. The lack of this information reflects, at least in part, the limited knowledge about the structural basis of antigen mimicry by anti-id antibodies and about the relationship between the extent of antigen mimicry and ability of a mimic to overcome unresponsiveness to a self-tumor antig...

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Alterations of protein synthesis in the cyanobacterium Synechocystis sp. PCC 6803 after a salt shock

Cited by 58 publications

References 20 publications

Effect of salinity on the biochemical composition of the alga Botryococcus braunii Kütz IPPAS H-252

Effect of salinity on the biochemical composition of the alga Botryococcus braunii Kütz IPPAS H-252

A fragment of the HMGN2 protein homes to the nuclei of tumor cells and tumor endothelial cells in vivo

Structural Basis of Antigen Mimicry in a Clinically Relevant Melanoma Antigen System

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