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53 Cards in this Set
- Front
- Back
What are bacteria? |
prokaryotes with ester linked membrane lipids, and peptidoglycan cell wall |
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Bacterial Shapes (morphology) |
Sperical (cocci) Rods (bacilli) filaments curved rods (vibrios) spirals (spiralla and spirochaetes) mycelia (branched filaments) |
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Strictly aerobic? |
NEED o2 |
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microaerophilic? |
need O2 at low levels |
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facultatively anaerobic? |
will use O2 if present |
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aerotolerant? |
can live in aerobic but do not use O2 |
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strictly anaerobic? |
killed by o2 |
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Gram staining technique? |
stain with crystal violet, fix with I2, destain with alcohol, counter stain with fuschin purple- gram pos (retain dye) pink- gram neg (didn't retain dye and stained by fuschin) |
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Genus Streptococcus info?. |
gram positive cocci in chains/ pairs facultatively anaerobic found on human membranes |
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Oral Streptococcus? |
S. mutans and S. salivarius colonise teeth, convert sucrose to dextron capsule use dextrin to adhere to teeth surface there they ferment sugars to lactic acid -> tooth decay |
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Pneumonia/ Meningitis causing Strep?. |
S. pneumoniae usually cocci pairs with polysaccharide capsule as main virulence factor alpha haemolytic |
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Genus Staphylococcus info?. |
gram positive facultatively anaerobic cocci in clusters skin and mucosal membranes |
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Staphylococcus aureus? |
Invades wounds=> 2ndry pneumonia, food poisoning, scalded skin syndrome, TSS develops resistance very well |
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VRSA and MRSA? |
vancomycin resistant S. aureus methicillin resistant S. aureus |
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Gram negative bact. eg? |
Salmonella typhi - typhoid Legionella pneumophila -legionnaires |
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Acid fast bacteria? |
Mycobacterium- aerobic rods with waxy lipid coating large amount of mycolic acids (lipid) in cell wall that resist gram staining, identify with Ziehl Neelson- red with blue back ground |
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Example of acid fast bacteria? |
Mycobacterium bovis, M. tuberculosis M. leprae |
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Enderospores? |
dormant non reproductive structure produced by some bacteria survive 1000s years, resistant to heat, production triggered by adverse conditions |
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Formation of enderospores? |
Bacteria undergoes asymmetrical cell division Spore produces Ca- dipicolinate (=> dehydration and inc. heat resistance) and small sol. proteins to protect DNA, ribosomes etc. "mother" secretes protein coat to protect spore then lyses and releases them |
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Examples of spore forming? |
Clostridium botulinum, C. tetani, C. perfringens, C. difficile, Bacillius antracis |
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Bacterial cell wall? |
Composed of peptidoglycan
polysacch, chains with peptide crosslinks
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Peptidoglycan structure? |
Alternating N-acetyl glucosamine and N-acetyl- muramic gram pos. = 20-25 layers gram neg.= 1-3 layers Nam residue= site for Beta lactams (a type of anti bio) binding |
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Arrangement of PDG in gram negative? |
the PDG polysacch chains wrapped around circ. of cell with peptide links parallel to axis |
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Arrangement of PDG in gram positive? |
polysacch. chain wound into cable and wrapped around cell |
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Lipopolysaccharide? |
outter part of outer membrane therefore only on gram negative Lipid A- 4/6 3 hydroxy fatty acids attached to a dimer of glucose amine phosphate (on membrane side) Core polysaccharide- fairly conserved linker 8,7 and 6 carbon sugar O-polysaccharide- 4-6 sugars repeated 10/20 times. Hydrophilic- repels phobic mol |
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Which specificity and toxicity of LPS? |
O- polysacch. varies and is highly strain specific (somatic antigen) Lipid A- causes fever (endotoxin) |
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Good antibiotics for LPS (neg. bac)? |
Polymixins- disrupt LPS |
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Bacterial capsules? . |
amorphouse polysaccharide slime secreted by bacteria to surrounding cells, forming tight matrix presence and composition is strain specific roles- prevent desiccation, inhibit phagocytosis ( e.g. streptococcus pneumoniae), attachment to surfaces (e.g. oral streptococci) |
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Bacterial flagella? |
used to move through liquids particularly common arrangement and number is strain specific 20nm in diameter recognised by immune system |
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Flagella Structure? |
Hollow filaments made of flagellin attached via hook to membranes L- ring attached to outer memo (neg. only) P- ring in PDG layer MS ring in cell membrane- with motor and switch proteins |
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How does flagella cause movement? |
generates thrust by rotating 200-1000 rpm M protein produces energy- ATP switch protein controls direction of rotation |
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Bacterial Pili and Fimbriae |
protein spikes used for attachment- shorter than flagella lots of fimbriae, few pili pili- DNA transfer in conjugation |
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Type 1 Fimbriae? |
Used by E.coli to adhere to urethra-> UTI |
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Bacterial Swarming? |
move in large groups along surface use flagella- often multiple lateral formation a.g. Bacillus |
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Bacterial twitching? |
Retractable polar Type 4 pili e.g. Pseudomonas, pili attached to substrate or other bacteria, and then contracts to pull forward |
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Bacterial gliding?> |
occurs in filamentous bacteria which don't swim e.g. Myxococcus |
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What do bacterial walls let through? |
Cytoplasmic membrane- perm barrier PDG- allows small molecules Outter membrane- repels H. phobic but allows small phillic through porins |
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Bacterial passive transport across memb ? |
relies on conc. gradient simple diffusion- small phobic mol. (gram pos) facilitated diffusion- phillic mol. through channel/ carrier protein. e.g. E.coli GlpF transporter to transport glycerol |
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Bacterial Active transport Proton symport? |
Driven by transmembrane proton gradient, where 1 or more protons enters with substrate e.g. E.coli lactose permease, LacY |
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Bacterial active transport ABC proteins? |
ATP binding casette transporters driven by ATP hydrolysis, assoc. with periplasmic substrate binding proteins |
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Maltose transport in E.coli |
ABC Maltose transporter (MalFG assoc. with MalK) MalK hydrolyses ATP-> ADP and Pi MalFGK transport maltose into cell which is assoc. with periplasmic binding protein MalE |
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Active transport in Bact Group translocation? |
substrate modified, generally phosphorylated, during transport saves an ATP as 1st step of glycolysis requires phosphorylation anyway |
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Glucose uptake in E.coli |
Group translocation PEP-> pyruvate, phosphate passed along system via enzymes chain (2a,2b and 2c are specific to substrate) end of chain stim. glucose to cross memb. and it phosphorylated to glucose-6-phosphate in the process |
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Crossing the outer membrane? |
Gram negative only Porins allow free diffusion of small phillic mol. Some substances can be actively moved using energy derived from cyto. memo. proton gradient, energy passed to channel/ carrier on OM via TonB |
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Outer membrane active transport example? |
On cytoplasmic membrane ExbBD gains energy by proton gradient Passes energy through TonB to BtuB transporter BtuB transport B12 across OM into periplasm |
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Secreting small molecules from bacteria? |
e.g. antibiotics, siderophores etc. Uses ABC transporter or proton antiporter |
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Secretion of proteins from bacteria? type 1 |
each target has on ABC transporter
exported across CM and OM using membrane fusion protein and outer memb. protein use energy from hydrolysing ATP |
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Example of type 1? |
E.coli haemolysin secretion HlyA recognised by region in C terminal of transporter protein, ATP hydrolysed and energy used to transport HlyA by HlyD, HlyB and TolC transporters |
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Secretion of proteins Type 2 |
Proteins to be exported from periplasm are recognised Pore is formed from subunits of protein D like a retractable type 4 pili, assembled like a piston and pushed protein out for extracellular hydrolytic enzymes |
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Secretion of proteins type 3? |
Injectisome assoc. with extracellular needle complex to insert across membrane of host cells |
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Type 3 secretion example? |
E.coli (enteropathogeniic strains) use to inject translocated intimin receptor in to cell membrane, so can use their own intimin to bind to it |
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Type 4 protein secretion? |
related to machinery used to export DNA: protein complexes during conjugation Used by heliobacter pylori, Boretella pertussis |
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General Secretion Pathway form bacteria? |
target identified by N terminal sequence on signal chaperoned by SecB or signal recognition particle, fed through Pore SecYEG into periplasm (in unfolded state) energy from SecATPase and proton channel SecDF in periplasm Lep removes lead peptide and protein unfolds. |