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53 Cards in this Set

  • Front
  • Back

What are bacteria?

prokaryotes with ester linked membrane lipids, and peptidoglycan cell wall

Bacterial Shapes (morphology)

Sperical (cocci)


Rods (bacilli)


filaments


curved rods (vibrios)


spirals (spiralla and spirochaetes)


mycelia (branched filaments)

Strictly aerobic?

NEED o2

microaerophilic?

need O2 at low levels

facultatively anaerobic?

will use O2 if present

aerotolerant?

can live in aerobic but do not use O2

strictly anaerobic?

killed by o2

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)

Genus Streptococcus info?.

gram positive


cocci in chains/ pairs


facultatively anaerobic


found on human membranes

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

Pneumonia/ Meningitis causing Strep?.

S. pneumoniae


usually cocci pairs


with polysaccharide capsule as main virulence factor


alpha haemolytic

Genus Staphylococcus info?.

gram positive


facultatively anaerobic


cocci in clusters


skin and mucosal membranes

Staphylococcus aureus?

Invades wounds=> 2ndry pneumonia, food poisoning, scalded skin syndrome, TSS


develops resistance very well

VRSA and MRSA?

vancomycin resistant S. aureus


methicillin resistant S. aureus

Gram negative bact. eg?

Salmonella typhi - typhoid


Legionella pneumophila -legionnaires

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

Example of acid fast bacteria?

Mycobacterium bovis, M. tuberculosis


M. leprae

Enderospores?

dormant non reproductive structure produced by some bacteria


survive 1000s years, resistant to heat, production triggered by adverse conditions

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

Examples of spore forming?

Clostridium botulinum, C. tetani, C. perfringens, C. difficile, Bacillius antracis

Bacterial cell wall?

Composed of peptidoglycan

polysacch, chains with peptide crosslinks




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

Arrangement of PDG in gram negative?

the PDG polysacch chains wrapped around circ. of cell with peptide links parallel to axis

Arrangement of PDG in gram positive?

polysacch. chain wound into cable and wrapped around cell

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

Which specificity and toxicity of LPS?

O- polysacch. varies and is highly strain specific


(somatic antigen)


Lipid A- causes fever (endotoxin)

Good antibiotics for LPS (neg. bac)?

Polymixins- disrupt LPS

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)

Bacterial flagella?

used to move through liquids


particularly common


arrangement and number is strain specific


20nm in diameter


recognised by immune system

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

How does flagella cause movement?

generates thrust by rotating 200-1000 rpm


M protein produces energy- ATP


switch protein controls direction of rotation

Bacterial Pili and Fimbriae


protein spikes used for attachment- shorter than flagella


lots of fimbriae, few pili


pili- DNA transfer in conjugation

Type 1 Fimbriae?

Used by E.coli to adhere to urethra-> UTI

Bacterial Swarming?

move in large groups along surface


use flagella- often multiple lateral formation


a.g. Bacillus

Bacterial twitching?

Retractable polar Type 4 pili


e.g. Pseudomonas, pili attached to substrate or other bacteria, and then contracts to pull forward

Bacterial gliding?>

occurs in filamentous bacteria which don't swim


e.g. Myxococcus

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

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

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

Bacterial active transport


ABC proteins?

ATP binding casette transporters


driven by ATP hydrolysis, assoc. with periplasmic substrate binding proteins



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

Active transport in Bact


Group translocation?

substrate modified, generally phosphorylated, during transport


saves an ATP as 1st step of glycolysis requires phosphorylation anyway

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

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

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

Secreting small molecules from bacteria?

e.g. antibiotics, siderophores etc.


Uses ABC transporter or proton antiporter

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





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

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

Secretion of proteins type 3?

Injectisome


assoc. with extracellular needle complex to insert across membrane of host cells



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

Type 4 protein secretion?

related to machinery used to export DNA: protein complexes during conjugation


Used by heliobacter pylori, Boretella pertussis

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.