Vancomycin is indicated for the treatment of serious, life-threatening infections byGram-positive bacteria of bothaerobic andanaerobic types[16] that are unresponsive to other antibiotics.[17][18][19]
The increasing emergence ofvancomycin-resistant enterococci (VRE) has resulted in the development of guidelines for use by theCenters for Disease Control Hospital Infection Control Practices Advisory Committee. These guidelines restrict use of vancomycin to these indications:[20][21]
treatment of infections in individuals with serious allergy topenicillins,
treatment ofpseudomembranous colitis caused byC. difficile; in particular, in cases of relapse or where the infection is unresponsive tometronidazole treatment (for this indication, vancomycin is given orally rather than intravenously),
treatment of infections caused by Gram-positive microorganisms in patients with serious allergies to beta-lactam antimicrobials,[21]
antibacterial prophylaxis forendocarditis after certain procedures in penicillin-hypersensitive people at high risk,[21]
surgical prophylaxis for major procedures involving implantation ofprostheses in institutions with a high rate of MRSA or MRSE,[21]
early in treatment as anempiric antibiotic for possible MRSA infection while waiting for culture identification of the infecting organism,
halting the progression ofprimary sclerosing cholangitis and preventing symptoms; vancomycin does not cure the patient and success is limited,
treatment ofendophthalmitis by intravitreal injection forGram-positive bacteria coverage;[22] it has been used to prevent the condition but is not recommended due to the risk of side effects.[23]
Although once described as narrow-spectrum,[25] numerous studies[26][27] have now shown that vancomycin decreases the levels of a wide spectum of bacteria, including members of theGram-negativeBacteroidota that are important in thehuman gut.
Serum vancomycin levels may be monitored in an effort to reduce side effects,[29] but the value of such monitoring has been questioned.[30] Peak and trough levels are usually monitored, and for research purposes the area under the concentration curve is also sometimes used.[31] Toxicity is best monitored by looking at trough values.[31] Immunoassays are commonly used to measure vancomycin levels.[29]
Commonadverse drug reactions (≥1% of patients) associated with intravenous vancomycin include:
pain, redness, or swelling at the injection site;[32]
vancomycin flushing syndrome (VFS), previously known asred man syndrome (or "redman syndrome");[28]
thrombophlebitis, which is common when administered through peripheral catheters but not when central venous catheters are used, although central venous catheters are a predisposing factor for upper-extremity deep-vein thrombosis.[33]
Damage to the kidneys (nephrotoxicity) and to the hearing (ototoxicity) were side effects of the early, impure versions of vancomycin, and were prominent in clinical trials conducted in the mid-1950s.[13][34] Later trials using purer forms of vancomycin foundnephrotoxicity is an infrequent adverse effect (0.1% to 1% of patients), but this is accentuated in the presence ofaminoglycosides.[35]
Historically, vancomycin has been considered a nephrotoxic and ototoxic drug, based on numerous case reports in the medical literature following initial approval by the FDA in 1958. But as its use increased with the spread of MRSA beginning in the 1970s, toxicity risks were reassessed. With the removal of impurities present in earlier formulations of the drug,[13] and with the introduction oftherapeutic drug monitoring, the risk of severe toxicity has been reduced.
The extent of nephrotoxicity for vancomycin remains controversial.[38] In 1980s, vancomycin with a purity > 90% was available, and kidney toxicity defined by an increase in serum creatinine of at least 0.5 mg/dL occurred in only about 5% of patients.[38] But dosing guidelines from the 1980s until 2008 recommended vancomycin trough concentrations between 5 and 15 μg/mL.[39] Concern for treatment failures prompted recommendations for higher dosing (troughs 15 to 20 μg/mL) for serious infection, and acute kidney injury (AKI) rates attributable to the vancomycin increased.[40]
Importantly, the risk of AKI increases with co-administration of other known nephrotoxins, in particular aminoglycosides. Furthermore, the sort of infections treated with vancomycin may also cause AKI, and sepsis is the most common cause of AKI in critically ill patients. Finally, studies in humans are mainly associations studies, where the cause of AKI is usually multifacotorial.[41][42][43][44]
Animal studies have demonstrated that higher doses and longer duration of vancomycin exposure correlates with increased histopathologic damage and elevations in urinary biomarkers of AKI.37-38[45] Damage is most prevalent at the proximal tubule, which is further supported by urinary biomarkers, such as kidney injury molecule-1 (KIM-1), clusterin, and osteopontin (OPN).[46] In humans, insulin-like growth factor binding protein 7 (IGFBP7) as part of the nephrocheck test.[47]
The mechanisms underlying the pathogenesis of vancomycin nephrotoxicity are multifactorial but include interstitial nephritis, tubular injury due to oxidative stress, and cast formation.[40]
Therapeutic drug monitoring can be used during vancomycin therapy to minimize the risk of nephrotoxicity associated with excessive drug exposure. Immunoassays are commonly utilized for measuring vancomycin levels.[29]
In children, concomitant administration of vancomycin andpiperacillin/tazobactam has been associated with an elevated incidence of AKI relative to other antibiotic regimens.[48]
Attempts to establish rates of vancomycin-inducedototoxicity are even more difficult due to lack of good data. The consensus is that clearly related cases of vancomycin ototoxicity are rare.[49][50] The association between vancomycin serum levels and ototoxicity is also uncertain. Cases of ototoxicity have been reported in patients whose vancomycin serum level exceeded 80 μg/mL,[51] but cases have also been reported in patients with therapeutic levels. Thus it remains unknown whethertherapeutic drug monitoring of vancomycin for the purpose of maintaining "therapeutic" levels prevents ototoxicity.[51] Still, therapeutic drug monitoring can be used during vancomycin therapy to minimize the risk of ototoxicity associated with excessive drug exposure.[29]
Another area of controversy and uncertainty is whether and to what extent vancomycin increases the toxicity of other nephrotoxins. Clinical studies have yielded various results, but animal models indicate that the nephrotoxic effect probably increases when vancomycin is added to nephrotoxins such as aminoglycosides. A dose- or serum level-effect relationship has not been established.[citation needed]
Vancomycin Flushing Reaction (aka "Red man syndrome")
Vancomycin is recommended to be administered in a dilute solution slowly, over at least 60 min (maximum rate of 10 mg/min for doses >500 mg)[20] due to the high incidence of pain and thrombophlebitis and to avoid an infusion reaction known as vancomycin flushing reaction. This phenomenon has been often clinically referred to as "red man syndrome". The reaction usually appears within 4 to 10 min after the commencement or soon after the completion of an infusion and is characterized by flushing and/or anerythematous rash that affects the face, neck, and upper torso, attributed to the release of histamine from mast cells. This reaction is caused by the interaction of vancomycin withMRGPRX2, a GPCR-mediating IgE-independent mast cell degranulation.[52] Less frequently,hypotension andangioedema occur. Symptoms may be treated or prevented withantihistamines, includingdiphenhydramine, and are less likely to occur with slow infusion.[53][54]
The recommended intravenous dosage in adults is 500 mg every 6 hours or 1000 mg every 12 hours, with modification to achieve a therapeutic range as needed. The recommended oral dosage in the treatment of antibiotic-induced pseudomembranous enterocolitis is 125 to 500 mg every 6 hours for 7 to 10 days.[55]
Dose optimization and target attainment of vancomycin in children involves adjusting the dosage to maximize effectiveness while minimizing the risk of adverse effects, specifically acute kidney injury. Dose optimization is achieved bytherapeutic drug monitoring (TDM), which allows measurement of vancomycin levels in the blood. TDM usingarea under the curve (AUC)-guided dosing, preferably with Bayesian forecasting, is recommended to ensure that the AUC0-24h/minimal inhibitory concentration (MIC) ratio is maintained above a certain threshold (400-600) associated with optimal efficacy.[56]
Vancomycin must be givenintravenously for systemic therapy since it is poorly absorbed from the intestine. It is a large hydrophilic molecule that partitions poorly across the gastrointestinalmucosa. Due to its short half-life, it is often injected twice daily.[57]
The only approved indication for oral vancomycin therapy is in the treatment of pseudomembranous colitis, where it must be given orally to reach the site of infection in the colon. After oral administration, the fecal concentration of vancomycin is around 500 μg/mL[58] (sensitive strains ofClostridioides difficile have a mean inhibitory concentration of ≤2 μg/mL[59])
Plasma level monitoring of vancomycin is necessary due to the drug's biexponential distribution, intermediate hydrophilicity, and potential for ototoxicity and nephrotoxicity, especially in populations with poor renal function and/or increased propensity to bacterial infection. Vancomycin activity is considered time-dependent; that is, antimicrobial activity depends on how long the serum drug concentration exceeds theminimum inhibitory concentration of the target organism. Thus, peak serum levels have not been shown to correlate with efficacy or toxicity; indeed, concentration monitoring is unnecessary in most cases. Circumstances in whichtherapeutic drug monitoring is warranted include patients receiving concomitant aminoglycoside therapy, patients with (potentially) alteredpharmacokinetic parameters, patients onhaemodialysis, patients administered high-dose or prolonged treatment, and patients with impaired renal function. In such cases, trough concentrations are measured.[20][30][66][67]
Therapeutic drug monitoring is also used for dose optimization of vancomycin in treating children.[56]
Target ranges for serum vancomycin concentrations have changed over the years. Early authors suggested peak levels of 30 to 40 mg/L andtrough levels of 5 to 10 mg/L,[68] but current recommendations are that peak levels need not be measured and thattrough levels of 10 to 15 mg/L or 15 to 20 mg/L, depending on the nature of the infection and the specific patient's needs, may be appropriate.[69][70] Measuring vancomycin concentrations to calculate doses optimizes therapy in patients withaugmented renal clearance.[71]
Vancomycin exhibitsatropisomerism—it has multiple chemically distinctrotamers owing to the rotational restriction of some of the bonds. The form present in the drug is the thermodynamically more stableconformer.[citation needed]
Figure 1: Modules and domains of vancomycin assembly
Vancomycin biosynthesis occurs primarily via threenonribosomal protein synthases (NRPSs) VpsA, VpsB, and VpsC.[72] Theenzymes determine the amino acid sequence during its assembly through its 7modules. Before vancomycin is assembled through NRPS, the non-proteinogenicamino acids are first synthesized.L-tyrosine is modified to become theβ-hydroxytyrosine (β-HT) and 4-hydroxyphenylglycine (4-Hpg) residues. 3,5-dihydroxyphenylglycine ring (3,5-DPG) is derived from acetate.[73]
Figure 2: Linear heptapeptide, which consists of modified aromatic rings
Nonribosomal peptide synthesis occurs through distinct modules that can load and extend theprotein by one amino acid per module through theamide bond formation at the contact sites of the activating domains.[74] Each module typically consists of anadenylation (A) domain, apeptidyl carrier protein (PCP) domain, and a condensation (C) domain. In the A domain, the specific amino acid is activated by converting into an aminoacyl adenylate enzyme complex attached to a4'-phosphopantetheine cofactor by thioesterification.[75][76] The complex is then transferred to the PCP domain with the expulsion of AMP. The PCP domain uses the attached 4'-phosphopantethein prosthetic group to load the growing peptide chain and their precursors.[77] The organization of the modules necessary to biosynthesize vancomycin is shown in Figure 1. In the biosynthesis of vancomycin, additional modification domains are present, such as theepimerization (E) domain, which isomerizes the amino acid from onestereochemistry to another, and a thioesterase domain (TE) is used as a catalyst for cyclization and releases of the molecule via athioesterase scission.[citation needed]
Figure 3: Modifications necessary for vancomycin to become biologically active
A set of NRPS enzymes (peptide synthase VpsA, VpsB, and VpsC) are responsible for assembling the heptapeptide. (Figure 2).[74] VpsA codes for modules 1, 2, and 3. VpsB codes for modules 4, 5, and 6, and VpsC codes for module 7. The vancomycin aglycone contains 4 D-amino acids, although the NRPSs only contain 3 epimerization domains. The origin of D-Leu at residue 1 is unknown. The three peptide syntheses are at the start of the region of the bacterial genome linked with antibiotic biosynthesis, and span 27 kb.[74]
β-hydroxytyrosine (β-HT) is synthesized before incorporation into the heptapeptide backbone. L-tyrosine is activated and loaded on the NRPS VpsD, hydroxylated by OxyD, and released by the thioesterase Vhp.[78] The timing of the chlorination by halogenase VhaA during biosynthesis is undetermined, but is proposed to occur before the complete assembly of the heptapeptide.[79]
After the linear heptapeptide molecule is synthesized, vancomycin must undergo further modifications, such as oxidative cross-linking andglycosylation, in trans[clarification needed] by distinct enzymes, referred to as tailoring enzymes, to become biologically active (Figure 3). To convert the linear heptapeptide to cross-linked, glycosylated vancomycin, six enzymes are required. The enzymes OxyA, OxyB, OxyC, and OxyD are cytochrome P450 enzymes. OxyB catalyzes oxidative cross-linking between residues 4 and 6, OxyA between residues 2 and 4, and OxyC between residues 5 and 7. This cross-linking occurs while the heptapeptide is covalently bound to the PCP domain of the 7th NRPS module. These P450s are recruited by the X domain in the 7th NRPS module, which is unique to glycopeptide antibiotic biosynthesis.[80] The cross-linked heptapeptide is then released by the action of the TE domain, and methyltransferase Vmt thenN-methylates the terminal leucine residue. GtfE then joins D-glucose to the phenolic oxygen of residue 4, followed by the addition ofvancosamine catalyzed by GtfD.[citation needed]
Some of the glycosyltransferases capable of glycosylating vancomycin and related nonribosomal peptides display notable permissivity and have been used to generate libraries of differentially glycosylated analogs throughglycorandomization.[81][82][83]
Both the vancomycinaglycone[84][85] and the complete vancomycin molecule[86] have been targets successfully reached bytotal synthesis. The target was first achieved by David Evans in October 1998, KC Nicolaou in December 1998, Dale Boger in 1999, and more selectively synthesized again by Boger in 2020.[84][87][88]
Crystal structure of a short peptideL-Lys-D-Ala-D-Ala (bacterial cell wall precursor, in green) bound to vancomycin (blue) throughhydrogen bonds[89]
Vancomycin targets bacterial cell wall synthesis by binding to the basic building block of the bacterial cell wall of Gram-positive bacteria, whether it is ofaerobic oranaerobic type.[16] Specifically, vancomycin forms hydrogen bonds with theD-alanyl-D-alanine (D-Ala-D-Ala) peptide motif of the peptidoglycan precursor, a component of the bacterial cell wall.[17]
Peptidoglycan is a polymer that provides structural support to the bacterial cell wall. The peptidoglycan precursor is synthesized in the cytoplasm and then transported across the cytoplasmic membrane to the periplasmic space, where it is assembled into the cell wall. The assembly process involves two enzymatic activities: transglycosylation and transpeptidation. Transglycosylation involves the polymerization of the peptidoglycan precursor into long chains, while transpeptidation involves the cross-linking of these chains to form a three-dimensional mesh-like structure.[17]
Vancomycin inhibits bacterial cell wall synthesis by binding to theD-Ala-D-Ala peptide motif of the peptidoglycan precursor, thereby preventing its processing by the transglycosylase; as such, vancomycin disrupts the transglycosylation activity of the cell wall synthesis process. The disruption leads to an incomplete and corrupted cell wall, which makes the replicating bacteria vulnerable to external forces such as osmotic pressure, so that the bacteria cannot survive and are eliminated by the immune system.[17]
Gram-negative bacteria are insensitive to vancomycin due to their different cell wall morphology. The outer membrane of Gram-negative bacteria contains lipopolysaccharide, which acts as a barrier to vancomycin penetration. That is why vancomycin is mainly used to treat infections caused by Gram-positive bacteria[17] (except some nongonococcal species ofNeisseria).[90][91]
The largehydrophilic molecule of vancomycin is able to formhydrogen bond interactions with the terminalD-alanyl-D-alanine moieties of the NAM/NAG-peptides. Under normal circumstances, this is a five-point interaction. This binding of vancomycin to theD-Ala-D-Ala prevents cell wall synthesis of the long polymers ofN-acetylmuramic acid (NAM) andN-acetylglucosamine (NAG) that form the backbone strands of the bacterial cell wall, and prevents the backbone polymers from cross-linking with each other.[92]
Mechanism of vancomycin action and resistance: This diagram shows only one of two ways vancomycin acts against bacteria (inhibition of cell wall cross-linking) and only one of many ways that bacteria can become resistant to it.
Vancomycin is added to the bacterial environment while it is trying to synthesize new cell wall. Here, the cell wall strands have been synthesized, but not yet cross-linked.
Vancomycin recognizes and binds to the twoD-ala residues on the end of the peptide chains. However, in resistant bacteria, the lastD-ala residue has been replaced by aD-lactate, so vancomycin cannot bind.
In the resistant bacteria, cross-links are successfully formed; still, in the nonresistant (sensitive) bacteria, the vancomycin bound to the peptide chains prevents them from interacting properly with the cell wall cross-linking enzyme.
In the resistant bacteria, stable cross-links are formed. In the sensitive bacteria, cross-links cannot be formed and the cell wall falls apart.
Vancomycin is one of the few antibiotics used in plant tissue culture to eliminate Gram-positive bacterial infection. It has relatively low toxicity to plants.[93][94]
Most Gram-negative bacteria are intrinsically resistant to vancomycin because their outer membranes are impermeable to large glycopeptide molecules[100] (with the exception of some non-gonococcalNeisseria species).[101]
Evolution ofmicrobial resistance to vancomycin is a growing problem, especially in healthcare facilities such as hospitals. While newer alternatives to vancomycin exist, such aslinezolid (2000) anddaptomycin (2003), the widespread use of vancomycin makes resistance to it a significant worry, especially for individual patients if resistant infections are not quickly identified and the patient continues an ineffective treatment.Vancomycin-resistantEnterococcus emerged in 1986.[102] Vancomycin resistance evolved in more common pathogenic organisms during the 1990s and 2000s, includingvancomycin-intermediateS. aureus (VISA) andvancomycin-resistantS. aureus (VRSA).[103][104] Agricultural use ofavoparcin, another similar glycopeptide antibiotic, may have contributed to the evolution of vancomycin-resistant organisms.[105][106][107][108]
One mechanism of resistance to vancomycin involves the alteration to the terminal amino acid residues of theNAM/NAG-peptide subunits, under normal conditions,D-alanyl-D-alanine, to which vancomycin binds. TheD-alanyl-D-lactate variation results in the loss of one hydrogen-bonding interaction (4, as opposed to 5 forD-alanyl-D-alanine) possible between vancomycin and the peptide. This loss of just one point of interaction results in a 1000-fold decrease in affinity. TheD-alanyl-D-serine variation causes a six-fold loss of affinity between vancomycin and the peptide, likely due tosteric hindrance.[109]
In enterococci, this modification appears to be due to the expression of an enzyme that alters the terminal residue. Three main resistance variants have been characterised to date among resistantEnterococcus faecium andE. faecalis populations:
VanA - enterococcal resistance to vancomycin andteicoplanin; inducible on exposure to these agents
VanB - lower-level enterococcal resistance; inducible by vancomycin, but strains may remain susceptible to teicoplanin
VanC - least clinically important; enterococci resistant only to vancomycin; constitutive resistance
A variant of vancomycin has been tested that binds to the resistant D-lactic acid variation in vancomycin-resistant bacterial cell walls and also binds well to the original target (vancomycin-susceptible bacteria).[110][111]
In 2020 a team at theUniversity Hospital Heidelberg (Germany) regained vancomycin's antibacterial power by modifying the molecule with a cationicoligopeptide. The oligopeptide consists of sixarginin units in Position VN. In comparison to the unmodified vancomycin the activity against vancomycin-resistant bacteria could be enhanced by a factor of 1,000.[112][113] This pharmacon is still inpreclinical development.
Vancomycin was first isolated in 1953 byEdmund Kornfeld (working atEli Lilly) from a bacteria in a soil sample collected from the interior jungles ofBorneo by a missionary, William M. Bouw.[114] The organism that produced it was eventually namedAmycolatopsis orientalis.[13] The original indication for vancomycin was to treat penicillin-resistantStaphylococcus aureus.[13][34]
The compound was initially called compound 05865, but was later given the generic name vancomycin, derived from the term "vanquish".[13] One quickly apparent advantage was that staphylococci did not develop significant resistance, despite serial passage in culture media containing vancomycin. The rapid development of penicillin resistance by staphylococci led to its being fast-tracked for approval by theFood and Drug Administration. In 1958, Eli Lilly first marketed vancomycin hydrochloride under the trade name Vancocin.[34]
Vancomycin never became the first-line treatment forS. aureus for several reasons:
It possesses poor oral bioavailability, so must be given intravenously for most infections.
β-Lactamase-resistant semisynthetic penicillins such asmethicillin (and its successors,nafcillin andcloxacillin) were subsequently developed, which have better activity against non-MRSA staphylococci.
Early trials used early, impure forms of the drug ("Mississippi mud"), which were found to be toxic to theinner ear and to the kidneys;[115] these findings led to the relegation of vancomycin to a drug of last resort.[34]
In 2004, Eli Lilly licensed Vancocin toViroPharma in the U.S., Flynn Pharma in the UK, andAspen Pharmacare in Australia. Thepatent expired in the early 1980s, and the FDA authorized the sale of several generic versions in the U.S., including from manufacturers Bioniche Pharma,Baxter Healthcare,Sandoz,Akorn-Strides, andHospira.[116]
The combination of vancomycin powder and povidone-iodine lavage may reduce the risk of periprosthetic joint infection in hip and knee arthroplasties.[117]
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